Current Research in Structural Biology最新文献

{"title":"The impact of SARS-CoV-2 spike mutation on peptide presentation is HLA allomorph-specific","authors":"You Min Ahn ,&nbsp;Janesha C. Maddumage ,&nbsp;Emma J. Grant ,&nbsp;Demetra S.M. Chatzileontiadou ,&nbsp;W.W.J. Gihan Perera ,&nbsp;Brian M. Baker ,&nbsp;Christopher Szeto ,&nbsp;Stephanie Gras","doi":"10.1016/j.crstbi.2024.100148","DOIUrl":"https://doi.org/10.1016/j.crstbi.2024.100148","url":null,"abstract":"<div><p>CD8⁺ T cells are crucial for viral elimination and recovery from viral infection. Nonetheless, the current understanding of the T cell response to SARS-CoV-2 at the antigen level remains limited. The Spike protein is an external structural protein that is prone to mutations, threatening the efficacy of current vaccines. Therefore, we have characterised the immune response towards the immunogenic Spike-derived peptide (S_976-984, VLNDILSRL), restricted to the HLA-A*02:01 molecule, which is mutated in both Alpha (S982A) and Omicron BA.1 (L981F) variants of concern. We determined that the mutation in the Alpha variant (S982A) impacted both the stability and conformation of the peptide, bound to HLA-A*02:01, in comparison to the original S_976-984. We identified a longer and overlapping immunogenic peptide (S_975-984, SVLNDILSRL) that could be presented by HLA-A*02:01, HLA-A*11:01 and HLA-B*13:01 allomorphs. We showed that S975-specific CD8⁺ T cells were weakly cross-reactive to the mutant peptides despite their similar conformations when presented by HLA-A*11:01. Altogether, our results show that the impact of SARS-CoV-2 mutations on peptide presentation is HLA allomorph-specific, and that post vaccination there are T cells able to react and cross-react towards the variant of concern peptides.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100148"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000254/pdfft?md5=68e3219bc99c70680b9c5efa9ff8b0ce&pid=1-s2.0-S2665928X24000254-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140824840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V","authors":"Y. Zenmei Ohkubo ,&nbsp;Peter W. Radulovic ,&nbsp;Albert N. Kahira ,&nbsp;Jesper J. Madsen","doi":"10.1016/j.crstbi.2024.100149","DOIUrl":"https://doi.org/10.1016/j.crstbi.2024.100149","url":null,"abstract":"<div><p>Anchoring of coagulation factors to anionic regions of the membrane involves the C2 domain as a key player. The rate of enzymatic reactions of the coagulation factors is increased by several orders of magnitude upon membrane binding. However, the precise mechanisms behind the rate acceleration remain unclear, primarily because of a lack of understanding of the conformational dynamics of the C2-containing factors and corresponding complexes. We elucidate the membrane-bound form of the C2 domain from human coagulation factor V (FV–C2) by characterizing its membrane binding the specific lipid-protein interactions. Employing all-atom molecular dynamics simulations and leveraging the highly mobile membrane-mimetic (HMMM) model, we observed spontaneous binding of FV-C2 to a phosphatidylserine (PS)-containing membrane within 2–25 ns across twelve independent simulations. FV-C2 interacted with the membrane through three loops (spikes 1–3), achieving a converged, stable orientation. Multiple HMMM trajectories of the spontaneous membrane binding provided extensive sampling and ample data to examine the membrane-induced effects on the conformational dynamics of C2 as well as specific lipid-protein interactions. Despite existing crystal structures representing presumed “open” and “closed” states of FV-C2, our results revealed a continuous distribution of structures between these states, with the most populated structures differing from both “open” and “closed” states observed in crystal environments. Lastly, we characterized a putative PS-specific binding site formed by K23, Q48, and S78 located in the groove enclosed by spikes 1–3 (PS-specificity pocket), suggesting a different orientation of a bound headgroup moiety compared to previous proposals based upon analysis of static crystal structures.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100149"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000266/pdfft?md5=e8ab6e6a13338f75043488820ca37b17&pid=1-s2.0-S2665928X24000266-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140879519","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor","authors":"Anindita Das ,&nbsp;Arpan Bysack ,&nbsp;H. Raghuraman","doi":"10.1016/j.crstbi.2024.100137","DOIUrl":"https://doi.org/10.1016/j.crstbi.2024.100137","url":null,"abstract":"<div><p>KvAP is a prokaryotic Kv channel, which has been widely used as a model system to understand voltage- and lipid-dependent gating mechanisms. In phospholipid membranes, the KvAP-VSD adopts the activated/‘Up’ conformation, whereas the presence of non-phospholipids in membranes favours the structural transition to resting/‘Down’ state. The S3b-S4 paddle motif loop of KvAP-VSD is functionally important as this participates in protein-protein interactions and is the target for animal toxins. In this study, we have monitored the modulatory role of cholesterol – the physiologically-relevant non-phospholipid – on the organization and dynamics of the S3b-S4 loop of the isolated KvAP-VSD in membranes by site-directed fluorescence approaches using the environmental sensitivity of 7-nitrobenz-2-oxa-1,3-diazol-4-yl-ethylenediamine (NBD) fluorescence. Our results show that cholesterol alters the dynamic nature (rotational and hydration dynamics) of S3b-S4 loop in a segmental fashion, <em>i.e</em>., the residues 110 to 114 and 115 to 117 behave differently in the presence of cholesterol, which is accompanied by considerable change in conformational heterogeneity. Further, quantitative depth measurements using the parallax quenching method reveal that the sensor loop is located at the shallow interfacial region of cholesterol-containing membranes, suggesting that the sensor loop organization is not directly correlated with S4 helix movement. Our results clearly show that cholesterol-induced changes in bilayer properties may not be the predominant factor for the sensor loop's altered structural dynamics, but can be attributed to the conformational change of the KvAP-VSD in cholesterol-containing membranes. Overall, these results are relevant for gating mechanisms, particularly the lipid-dependent gating, of Kv channels in membranes.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100137"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X2400014X/pdfft?md5=4e693bf08aef23c565c35af77c0c3c70&pid=1-s2.0-S2665928X2400014X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140095959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria","authors":"Lumbini R. Yadav ,&nbsp;Vasudha Sharma ,&nbsp;Maheswaran Shanmugam ,&nbsp;Shekhar C. Mande","doi":"10.1016/j.crstbi.2024.100157","DOIUrl":"10.1016/j.crstbi.2024.100157","url":null,"abstract":"<div><div>Class I ribonucleotide reductases consisting of α and β subunits convert ribonucleoside diphosphates to deoxyribonucleoside diphosphates involving an intricate free radical mechanism. The generation of free radicals in the Class Ib ribonucleotide reductases is mediated by di-manganese ions in the β subunits and is externally assisted by flavodoxin-like NrdI subunit. This is unlike Class Ia ribonucleotide reductases, where the free radical generation is initiated at its di-iron centre in the β subunits with no external support from another subunit. Class 1b ribonucleotide reductase complex is an essential enzyme complex in the human pathogen <em>Mycobacterium tuberculosis</em> and its structural details are largely unknown. In this study we have determined the crystal structures of Mycobacterial NrdI in oxidised and reduced forms, and similarly those of NrdF2:NrdI complexes. These structures provide detailed atomic view of the mechanism of free radical generation in the β subunit in this pathogen. We observe a well-formed channel in NrdI from the surface leading to the buried FMN moiety and propose that oxygen molecule accesses FMN through it. The oxygen molecule is further converted to a superoxide ion upon electron transfer at the FMN moiety. Similarly, a path for superoxide radical transfer between NrdI and NrdF2 is also observed. The oxidation of Mn(II) in NrdF2I to high valent oxidation state (either Mn(III) or Mn(IV) assisted by the reduced FMN site was evidently confirmed by EPR studies. SEC-MALS and low resolution cryo-EM map indicate unusual stoichiometry of 2:1 in the <em>M. tuberculosis</em> NrdF2I complex. A density close to Tyr 110 at a distance &lt;2.3 Å is observed, which we interpret as OH group. Overall, the study therefore provides important clues on the initiation of free radical generation in the β subunit of the ribonucleotide reductase complex in <em>M. tuberculosis</em>.</div></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"8 ","pages":"Article 100157"},"PeriodicalIF":2.7,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142323032","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Conformational analysis of the IQSEC2 protein by statistical thermodynamics","authors":"Michael Shokhen ,&nbsp;Amnon Albeck ,&nbsp;Veronika Borisov ,&nbsp;Yonat Israel ,&nbsp;Nina S. Levy ,&nbsp;Andrew P. Levy","doi":"10.1016/j.crstbi.2024.100158","DOIUrl":"10.1016/j.crstbi.2024.100158","url":null,"abstract":"<div><div>Mutations in the IQSEC2 gene result in severe intellectual disability, epilepsy and autism. The primary function of IQSEC2 is to serve as a guanine exchange factor (GEF) controlling the activation of ARF6 which in turn mediates membrane trafficking and synaptic connections between neurons. As IQSEC2 is a large intrinsically disordered protein little is known of the structure of the protein and how this influences its function. Understanding this structure and function relationship is critical for the development of novel therapies to treat IQSEC2 disease. We therefore sought to identify IQSEC2 conformers in unfolded and folded states and analyze how conformers differ when binding to ARF6 and thereby influence GEF catalysis. We simulated the folding process of IQSEC2 by accelerated molecular dynamics (aMD). Following the ensemble method of Gibbs, we proposed that the number of microstates in the ensemble replicating a protein macroscopic system is the total number of MD snapshots sampled on the production MD trajectory. We divided the entire range of reaction coordinate into a series of consecutive, non-overlapping bins. Thermal fluctuations of biomolecules in local equilibrium states are Gaussian in form. To predict the free energy and entropy of different conformational states using statistical thermodynamics, the density of states was estimated taking into account how many MD snapshots constitute each conformational state. IQSEC2 dimers derived from the most stable folded and unfolded conformers of IQSEC2 were generated by protein-protein docking and then used to construct IQSEC2-ARF6 encounter complexes. We suggest that IQSEC2 folding and dimerization are two competing processes that may be used by nature to regulate the process of GDP exchange on ARF6 catalyzed by IQSEC2.</div></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"8 ","pages":"Article 100158"},"PeriodicalIF":2.7,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stability and dynamics of extradenticle modulates its function","authors":"Aakanksha Singh,&nbsp;Bidisha Acharya,&nbsp;Beas Mukherjee,&nbsp;Veda Sheersh Boorla ,&nbsp;Soumendu Boral ,&nbsp;Snigdha Maiti ,&nbsp;Soumya De","doi":"10.1016/j.crstbi.2024.100150","DOIUrl":"https://doi.org/10.1016/j.crstbi.2024.100150","url":null,"abstract":"<div><p>Extradenticle (EXD) is a partner protein of the HOX transcription factors and plays an important role in the development of Drosophila. It confers increased affinity and specificity of DNA-binding to the HOX proteins. However, the DNA-binding homeodomain of EXD has a significantly weaker affinity to DNA compared to the HOX homeodomains. Here, we show that a glycine residue (G290) in the middle of the EXD DNA-binding helix primarily results in this weaker binding. Glycine destabilizes helices. To probe its role in the stability and function of the protein, G290 was mutated to alanine. The intrinsic stability of the DNA-binding helix increased in the G290A mutant as observed by NMR studies and molecular dynamics (MD) simulation. Also, NMR dynamics and MD simulation show that dynamic motions present in the wild-type protein are quenched in the mutant. This in turn resulted in increased stability of the entire homeodomain (ΔΔG_G→A of −2.6 kcal/mol). Increased protein stability resulted in three-fold better DNA-binding affinity of the mutant as compared to the wild-type protein. Molecular mechanics with generalized Born and surface area solvation (MMGBSA) analysis of our MD simulation on DNA-bound models of both wild-type and mutant proteins shows that the contribution to binding is enhanced for most of the interface residues in the mutant compared to the wild-type. Interestingly, the flexible N-terminal arm makes more stable contact with the DNA minor groove in the mutant. We found that the two interaction sites i.e. the DNA-binding helix and the unstructured N-terminal arm influence each other via the bound DNA. These results provide an interesting conundrum: alanine at position 290 enhances both the stability and the DNA-binding affinity of the protein, however, evolution prefers glycine at this position. We have provided several plausible explanations for this apparent conundrum. The function of the EXD as a HOX co-factor requires its ability to discriminate similar DNA sequences, which is most likely comprom</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100150"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000278/pdfft?md5=fd7d76e526dba2e2fb02993ab8d46a86&pid=1-s2.0-S2665928X24000278-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140946903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"SAGESDA: Multi-GraphSAGE networks for predicting SnoRNA-disease associations","authors":"Biffon Manyura Momanyi ,&nbsp;Yu-Wei Zhou ,&nbsp;Bakanina Kissanga Grace-Mercure ,&nbsp;Sebu Aboma Temesgen ,&nbsp;Ahmad Basharat ,&nbsp;Lin Ning ,&nbsp;Lixia Tang ,&nbsp;Hui Gao ,&nbsp;Hao Lin ,&nbsp;Hua Tang","doi":"10.1016/j.crstbi.2023.100122","DOIUrl":"https://doi.org/10.1016/j.crstbi.2023.100122","url":null,"abstract":"<div><p>Over the years, extensive research has highlighted the functional roles of small nucleolar RNAs in various biological processes associated with the development of complex human diseases. Therefore, understanding the existing relationships between different snoRNAs and diseases is crucial for advancing disease diagnosis and treatment. However, classical biological experiments for identifying snoRNA-disease associations are expensive and time-consuming. Therefore, there is an urgent need for cost-effective computational techniques that can enhance the efficiency and accuracy of prediction. While several computational models have already been proposed, many suffer from limitations and suboptimal performance. In this study, we introduced a novel Graph Neural Network-based (GNN) classification model, called SAGESDA, which is implemented through the GraphSAGE architecture with attention for the prediction of snoRNA-disease associations. The classifier leverages local neighbouring nodes in a heterogeneous network to generate new node embeddings through message passing. The mini-batch gradient descent technique was applied to divide the graph into smaller sub-graphs, which enhances the model's accuracy, speed and scalability. With these advancements, SAGESDA attained an area under the receiver operating characteristic (ROC) curve (AUC) of 0.92 using the standard dot product classifier, surpassing previous related studies. This notable performance demonstrates that SAGESDA is a promising model for predicting unknown snoRNA-disease associations with high accuracy. The SAGESDA implementation details can be obtained from <span>https://github.com/momanyibiffon/SAGESDA.git</span><svg><path></path></svg>.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100122"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000284/pdfft?md5=53e908984f68e8f4f39afb0050a896ca&pid=1-s2.0-S2665928X23000284-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139107210","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioinformatic analysis of THAP9 transposase homolog: conserved regions, novel motifs","authors":"Richa Rashmi ,&nbsp;Chandan Nandi ,&nbsp;Sharmistha Majumdar","doi":"10.1016/j.crstbi.2023.100113","DOIUrl":"10.1016/j.crstbi.2023.100113","url":null,"abstract":"<div><p>THAP9 is a transposable element-derived gene that encodes the THAP9 protein, which is homologous to the <em>Drosophila</em> P-element transposase (DmTNP) and can cut and paste DNA. However, the exact functional role of THAP9 is unknown. Here, we perform structure prediction, evolutionary analysis and extensive <em>in silico</em> characterization of THAP9, including predicting domains and putative post-translational modification sites. Comparison of the AlphaFold-predicted structure of THAP9 with the DmTNP CryoEM structure, provided insights about the C2CH motif and other DNA binding residues, RNase H-like catalytic domain and insertion domain of the THAP9 protein. We also predicted previously unreported mammalian-specific post-translational modification sites that may play a role in the subcellular localization of THAP9. Furthermore, we observed that there are distinct organism class-specific conservation patterns of key functional residues in certain THAP9 domains.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100113"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X23000193/pdfft?md5=c3c5880ce6446e6690c6b1d1b686feff&pid=1-s2.0-S2665928X23000193-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139293648","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Assessment of Kaistella jeonii esterase conformational dynamics in response to poly(ethylene terephthalate) binding","authors":"Ederson Sales Moreira Pinto ,&nbsp;Arthur Tonietto Mangini ,&nbsp;Lorenzo Chaves Costa Novo ,&nbsp;Fernando Guimaraes Cavatao ,&nbsp;Mathias J. Krause ,&nbsp;Marcio Dorn","doi":"10.1016/j.crstbi.2024.100130","DOIUrl":"10.1016/j.crstbi.2024.100130","url":null,"abstract":"<div><p>The pervasive presence of plastic in the environment has reached a concerning scale, being identified in many ecosystems. Bioremediation is the cheapest and most eco-friendly alternative to remove this polymer from affected areas. Recent work described that a novel cold-active esterase enzyme extracted from the bacteria <em>Kaistella jeonii</em> could promiscuously degrade PET. Compared to the well-known PETase from <em>Ideonella sakaiensis</em>, this novel esterase presents a low sequence identity yet has a remarkably similar folding. However, enzymatic assays demonstrated a lower catalytic efficiency. In this work, we employed a strict computational approach to investigate the binding mechanism between the esterase and PET. Understanding the underlying mechanism of binding can shed light on the evolutive mechanism of how enzymes have been evolving to degrade these artificial molecules and help develop rational engineering approaches to improve PETase-like enzymes. Our results indicate that this esterase misses a disulfide bridge, keeping the catalytic residues closer and possibly influencing its catalytic efficiency. Moreover, we describe the structural response to the interaction between enzyme and PET, indicating local and global effects. Our results aid in deepening the knowledge behind the mechanism of biological catalysis of PET degradation and as a base for the engineering of novel PETases.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100130"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000072/pdfft?md5=33dd0e45dffd911f763970f961540bfb&pid=1-s2.0-S2665928X24000072-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139889948","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and functional profile of phytases across the domains of life","authors":"Benjamin M. Scott ,&nbsp;Kevin Koh ,&nbsp;Gregory D. Rix","doi":"10.1016/j.crstbi.2024.100139","DOIUrl":"https://doi.org/10.1016/j.crstbi.2024.100139","url":null,"abstract":"<div><p>Phytase enzymes are a crucial component of the natural phosphorus cycle, as they help make phosphate bioavailable by releasing it from phytate, the primary reservoir of organic phosphorus in grain and soil. Phytases also comprise a significant segment of the agricultural enzyme market, used primarily as an animal feed additive. At least four structurally and mechanistically distinct classes of phytases have evolved in bacteria and eukaryotes, and the natural diversity of each class is explored here using advances in protein structure prediction and functional annotation. This graphical review aims to provide a succinct description of the major classes of phytase enzymes across phyla, including their structures, conserved motifs, and mechanisms of action.</p></div>","PeriodicalId":10870,"journal":{"name":"Current Research in Structural Biology","volume":"7 ","pages":"Article 100139"},"PeriodicalIF":2.8,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665928X24000163/pdfft?md5=ae60c1887f74c5107da5399729903531&pid=1-s2.0-S2665928X24000163-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140208889","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}