Proteins-Structure Function and Bioinformatics最新文献_第10页

On the pathway of the formation of secondary structures in proteins. 关于蛋白质二级结构形成的途径。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-09-23 DOI: 10.1002/prot.26591

Pinak Chakrabarti

{"title":"On the pathway of the formation of secondary structures in proteins.","authors":"Pinak Chakrabarti","doi":"10.1002/prot.26591","DOIUrl":"10.1002/prot.26591","url":null,"abstract":"Protein structures are typically made up of well-defined modules, called secondary structures. A hierarchical model of protein folding may start with the formation of five-membered non-covalently-linked ring motifs involving O⋅⋅⋅C=O and N-H···N interactions connecting two consecutive peptide groups. Some of these interactions lead to polyproline II structure, which are known to occur in the unfolded state of proteins. These interactions constitute different types of γ-turns, providing the sharpest reversal of the chain direction. Occurring transiently in the unfolded state, and in tandem, they can lead to β-turns. One of the β-turns (type I) is predisposed (from a consideration of residue usage) to form the N-terminal of an α-helix, which then propagates toward its C-terminal direction. O⋅⋅⋅C=O interactions encompass four distinct types of conformational features, and one of them has very similar backbone torsion angles as the polyproline II (PPII) conformation and can thus contribute to the formation of PPII helix. An adjustment from these angles can also drive the formation of β-strand. N-H···N interactions can also constitute capping interaction at helix termini and can link a PPII helix to an α-helix. Thus, the polypeptide backbone is endowed with all the features that can initiate the formation of secondary structural elements, and the γ-turn motifs (resulting from O⋅⋅⋅C=O and N-H···N interactions) are the basic units the protein structures are made up of.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"396-399"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41173530","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Atomic visualization of flipped-back conformations of high mannose glycans interacting with cargo lectins: An MD simulation perspective. 高甘露糖聚糖与货物凝集素相互作用的反翻构象的原子可视化：MD模拟视角。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-07-19 DOI: 10.1002/prot.26556

Nisha Grandhi Jayaprakash, Dheeraj Kumar Sarkar, Avadhesha Surolia

{"title":"Atomic visualization of flipped-back conformations of high mannose glycans interacting with cargo lectins: An MD simulation perspective.","authors":"Nisha Grandhi Jayaprakash, Dheeraj Kumar Sarkar, Avadhesha Surolia","doi":"10.1002/prot.26556","DOIUrl":"10.1002/prot.26556","url":null,"abstract":"Protein-carbohydrate interactions play a crucial role in mediating several biomolecular recognition events. We attempt to unravel its intricacies by understanding how carbohydrate-binding proteins interpret the glycan code. We aim to decipher lectin-mediated recognition in the endoplasmic reticulum (ER), which plays a crucial role in ER-mediated quality control (ER-QC). The ER-QC functions in three phases-protein folding, transport, and degradation. Altered protein QC leads to ER-related storage disorders. Cargo transport proteins-Ergic53 and Vip36-necessary for maintaining cellular homeostasis-are our primary focus. They recognize monoglucosylated/high mannose N-glycans on the folded glycoproteins. This article reports on the first dynamic investigation of the ER cargo lectins in complex with the high mannose glycans using an advanced sampling technique-replica exchange molecular dynamics to decipher the inherent conformational heterogeneity and the binding mechanism. The study involves simulations for the proteins complexed with three high mannose glycans-Man8B, Man9, and mono-glucosylated glycan. The recognition process is captured using MD simulations to achieve mechanistic insights and characterize the dynamics of glycans in their native and bound states via dihedral angle analysis. Results indicate that the flipped conformation of the glycans was crucial in differentiating their interaction with the proteins. Similar conformers of the glycans are preferred for Ergic53 and Vip36 in their glycan recognition events. Ergic53 preferred Man8B while it was Man9 for Vip36, in coherence with the previous experimental reports. These simulations provide a computational microscopic purview of the mechanism at both spatial and temporal scales. The results correlate with the published experimental data on the specificities of these lectins.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"112-133"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9834745","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Insights into the solution structure and transcriptional regulation of the MazE9 antitoxin in Mycobacterium tuberculosis. 结核分枝杆菌中MazE9抗毒素溶液结构和转录调控的见解。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-09-22 DOI: 10.1002/prot.26589

Tanaya Basu Roy, Siddhartha P Sarma

引用次数: 0

Identification of sequence determinants for the ABHD14 enzymes. ABHD14酶序列决定因素的鉴定。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-11-16 DOI: 10.1002/prot.26632

Kaveri Vaidya, Golding Rodrigues, Sonali Gupta, Archit Devarajan, Mihika Yeolekar, M S Madhusudhan, Siddhesh S Kamat

{"title":"Identification of sequence determinants for the ABHD14 enzymes.","authors":"Kaveri Vaidya, Golding Rodrigues, Sonali Gupta, Archit Devarajan, Mihika Yeolekar, M S Madhusudhan, Siddhesh S Kamat","doi":"10.1002/prot.26632","DOIUrl":"10.1002/prot.26632","url":null,"abstract":"Over the course of evolution, enzymes have developed remarkable functional diversity in catalyzing important chemical reactions across various organisms, and understanding how new enzyme functions might have evolved remains an important question in modern enzymology. To systematically annotate functions, based on their protein sequences and available biochemical studies, enzymes with similar catalytic mechanisms have been clustered together into an enzyme superfamily. Typically, enzymes within a superfamily have similar overall three-dimensional structures, conserved catalytic residues, but large variations in substrate recognition sites and residues to accommodate the diverse biochemical reactions that are catalyzed within the superfamily. The serine hydrolases are an excellent example of such an enzyme superfamily. Based on known enzymatic activities and protein sequences, they are split almost equally into the serine proteases and metabolic serine hydrolases. Within the metabolic serine hydrolases, there are two outlying members, ABHD14A and ABHD14B, that have high sequence similarity, but their biological functions remained cryptic till recently. While ABHD14A still lacks any functional annotation to date, we recently showed that ABHD14B functions as a lysine deacetylase in mammals. Given their high sequence similarity, automated databases often wrongly assign ABHD14A and ABHD14B as the same enzyme, and therefore, annotating functions to them in various organisms has been problematic. In this article, we present a bioinformatics study coupled with biochemical experiments, which identifies key sequence determinants for both ABHD14A and ABHD14B, and enable better classification for them. In addition, we map these enzymes on an evolutionary timescale and provide a much-wanted resource for studying these interesting enzymes in different organisms.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"255-266"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136400546","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Substrate selectivity and unique sequence signatures in SWEET/semiSWEET homologs of four taxonomic groups: Sequence analysis and phylogenetic studies. 四个分类群 SWEET/semiSWEET 同源物的底物选择性和独特序列特征：序列分析和系统发育研究。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2024-01-19 DOI: 10.1002/prot.26670

Ankita Gupta, Ramasubbu Sankararamakrishnan

{"title":"Substrate selectivity and unique sequence signatures in SWEET/semiSWEET homologs of four taxonomic groups: Sequence analysis and phylogenetic studies.","authors":"Ankita Gupta, Ramasubbu Sankararamakrishnan","doi":"10.1002/prot.26670","DOIUrl":"10.1002/prot.26670","url":null,"abstract":"The recently discovered SWEET (Sugar Will Eventually be Exported Transporter) proteins are involved in the selective transport of monosaccharides and disaccharides. The prokaryotic counterparts, semiSWEETs, form dimers with each monomer forming a triple-helix transmembrane bundle (THB). The longer eukaryotic SWEETs have seven transmembrane helices with two THBs and a linker helix. Structures of semiSWEETs/SWEETs have been determined experimentally. Experimental studies revealed the role of plant SWEETs in vital physiological processes and identified residues responsible for substrate selectivity. However, SWEETs/semiSWEETs from metazoans and bacteria are not characterized. In this study, we used structure-based sequence alignment and compared more than 2000 SWEET/semiSWEETs from four different taxonomic groups. Conservation of residue/chemical property was examined at all positions. Properties of clades/subclades of phylogenetic trees from each taxonomic group were analyzed. Conservation pattern of known residues in the selectivity-filter was used to predict the substrate preference of plant SWEETs and some clusters of metazoans and bacteria. Some residues at the gating and substrate-binding regions, pore-facing positions and at the helix-helix interface are conserved across all taxonomic groups. Conservation of polar/charged residues at specific pore-facing positions, helix-helix interface and in loops seems to be unique for plant SWEETs. Overall, the number of conserved residues is less in metazoan SWEETs. Plant and metazoan SWEETs exhibit high conservation of four and three proline residues respectively in \"proline tetrad.\" Further experimental studies can validate the predicted substrate selectivity and significance of conserved polar/charged/aromatic residues at structurally and functionally important positions of SWEETs/semiSWEETs in plants, metazoans and bacteria.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"320-340"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139503262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

sAMP-VGG16: Force-field assisted image-based deep neural network prediction model for short antimicrobial peptides. sAMP-VGG16：基于力场辅助图像的短抗菌肽深度神经网络预测模型。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2024-03-23 DOI: 10.1002/prot.26681

Poonam Pandey, Anand Srivastava

{"title":"sAMP-VGG16: Force-field assisted image-based deep neural network prediction model for short antimicrobial peptides.","authors":"Poonam Pandey, Anand Srivastava","doi":"10.1002/prot.26681","DOIUrl":"10.1002/prot.26681","url":null,"abstract":"During the last three decades, antimicrobial peptides (AMPs) have emerged as a promising therapeutic alternative to antibiotics. The approaches for designing AMPs span from experimental trial-and-error methods to synthetic hybrid peptide libraries. To overcome the exceedingly expensive and time-consuming process of designing effective AMPs, many computational and machine-learning tools for AMP prediction have been recently developed. In general, to encode the peptide sequences, featurization relies on approaches based on (a) amino acid (AA) composition, (b) physicochemical properties, (c) sequence similarity, and (d) structural properties. In this work, we present an image-based deep neural network model to predict AMPs, where we are using feature encoding based on Drude polarizable force-field atom types, which can capture the peptide properties more efficiently compared to conventional feature vectors. The proposed prediction model identifies short AMPs (≤30 AA) with promising accuracy and efficiency and can be used as a next-generation screening method for predicting new AMPs. The source code is publicly available at the Figshare server sAMP-VGG16.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"372-383"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140195206","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Computational analyses of drug resistance mutations in katG and emb complexes in Mycobacterium tuberculosis. 结核分枝杆菌中 katG 和 emb 复合物耐药性突变的计算分析。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2024-03-14 DOI: 10.1002/prot.26684

Aadam Basrai, Tom L Blundell, Arun Prasad Pandurangan

{"title":"Computational analyses of drug resistance mutations in katG and emb complexes in Mycobacterium tuberculosis.","authors":"Aadam Basrai, Tom L Blundell, Arun Prasad Pandurangan","doi":"10.1002/prot.26684","DOIUrl":"10.1002/prot.26684","url":null,"abstract":"The number of antibiotic resistant pathogens is increasing rapidly, and with this comes a substantial socioeconomic cost that threatens much of the world. To alleviate this problem, we must use antibiotics in a more responsible and informed way, further our understanding of the molecular basis of drug resistance, and design new antibiotics. Here, we focus on a key drug-resistant pathogen, Mycobacterium tuberculosis, and computationally analyze trends in drug-resistant mutations in genes of the proteins embA, embB, embC, and katG, which play essential roles in the action of the first-line drugs ethambutol and isoniazid. We use docking to predict binding modes of isoniazid to katG that agree with suggested binding sites found in our laboratory using cryo-EM. Using mutant stability predictions, we recapitulate the idea that resistance occurs when katG's heme cofactor is destabilized rather than due to a decrease in affinity to isoniazid. Conversely, we have identified resistance mutations that affect the affinity of ethambutol more drastically than the affinity of the natural substrate of embB. With this, we illustrate that we can distinguish between the two types of drug resistance-cofactor destabilization and drug affinity reduction-suggesting potential uses in the prediction of novel drug-resistant mutations.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"359-371"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11623437/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140121484","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Signatures of tRNA^Glx-specificity in proteobacterial glutamyl-tRNA synthetases. 蛋白质细菌谷氨酰trna合成酶中tRNAGlx特异性的特征。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-11-12 DOI: 10.1002/prot.26634

Saumya Dasgupta, Aditya Dev, Nipa Chongdar, Premananda Basak, Shubhra Ghosh Dastidar, Gautam Basu

{"title":"Signatures of tRNAGlx-specificity in proteobacterial glutamyl-tRNA synthetases.","authors":"Saumya Dasgupta, Aditya Dev, Nipa Chongdar, Premananda Basak, Shubhra Ghosh Dastidar, Gautam Basu","doi":"10.1002/prot.26634","DOIUrl":"10.1002/prot.26634","url":null,"abstract":"The canonical function of glutamyl-tRNA synthetase (GluRS) is to glutamylate tRNAGlu. Yet not all bacterial GluRSs glutamylate tRNAGlu; many glutamylate both tRNAGlu and tRNAGln, while some glutamylate only tRNAGln and not the cognate substrate tRNAGlu. Understanding the basis of the unique specificity of tRNAGlx is important. Mutational studies have hinted at hotspot residues, both on tRNAGlx and GluRS, which play crucial roles in tRNAGlx-specificity. However, its underlying structural basis remains unexplored. The majority of biochemical studies related to tRNAGlx-specificity have been performed on GluRS from Escherichia coli and other proteobacterial species. However, since the early crystal structures of GluRS and tRNAGlu-bound GluRS were from non-proteobacterial species (Thermus thermophilus), proteobacterial biochemical data have often been interpreted in the context of non-proteobacterial GluRS structures. Marked differences between proteobacterial and non-proteobacterial GluRSs have been demonstrated; therefore, it is important to understand tRNAGlx-specificity vis-a-vis proteobacterial GluRS structures. To this end, we solved the crystal structure of a double mutant GluRS from E. coli. Using the solved structure and several other currently available proteo- and non-proteobacterial GluRS crystal structures, we probed the structural basis of the tRNAGlx-specificity of bacterial GluRSs. Specifically, our analyses suggest a unique role played by the tRNAGlx D-helix contacting loop of GluRS in the modulation of tRNAGln-specificity. While earlier studies have identified functional hotspots on tRNAGlx that control the tRNAGlx-specificity of GluRS, this is the first report of complementary signatures of tRNAGlx-specificity in GluRS.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"241-254"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89720822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Comparison of structural networks across homologous proteins. 同源蛋白结构网络的比较。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-12-07 DOI: 10.1002/prot.26650

Vasam Manjveekar Prabantu, Vasundhara Gadiyaram, Saraswathi Vishveshwara, Narayanaswamy Srinivasan

{"title":"Comparison of structural networks across homologous proteins.","authors":"Vasam Manjveekar Prabantu, Vasundhara Gadiyaram, Saraswathi Vishveshwara, Narayanaswamy Srinivasan","doi":"10.1002/prot.26650","DOIUrl":"10.1002/prot.26650","url":null,"abstract":"Protein sequence determines its structure and function. The indirect relationship between protein function and structure lies deep-rooted in the structural topology that has evolved into performing optimal function. The evolution of structure and its interconnectivity has been conventionally studied by comparing the root means square deviation between protein structures at the backbone level. Two factors that are necessary for the quantitative comparison of non-covalent interactions are (a) explicit inclusion of the coordinates of side-chain atoms and (b) consideration of multiple structures from the conformational landscape to account for structural variability. We have recently addressed these fundamental issues by investigating the alteration of inter-residue interactions across an ensemble of protein structure networks through a graph spectral approach. In this study, we have developed a rigorous method to compare the structure networks of homologous proteins, with a wide range of sequence identity percentages. A range of dissimilarity measures that show the extent of change in the network across homologous structures are generated, which also includes the comparison of the protein structure variability. We discuss in detail, scenarios where the variation of structure is not accompanied by loss or gain of the overall network and its vice versa. The sequence-based phylogeny among the homologs is also compared with the lineage obtained from information from such a robust structure comparison. In summary, we can obtain a quantitative comparison score for the structure networks of homologous proteins, which also enables us to study the evolution of protein function based on the variation of their topologies.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"267-278"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138500359","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Initiation factor 3 bound to the 30S ribosomal subunit in an initial step of translation. 在翻译的初始步骤中，启动因子 3 与 30S 核糖体亚基结合。

IF 3.2 4区生物学

Proteins-Structure Function and Bioinformatics Pub Date : 2025-01-01 Epub Date: 2023-12-26 DOI: 10.1002/prot.26655

Adwaith B Uday, Rishi Kumar Mishra, Tanweer Hussain

{"title":"Initiation factor 3 bound to the 30S ribosomal subunit in an initial step of translation.","authors":"Adwaith B Uday, Rishi Kumar Mishra, Tanweer Hussain","doi":"10.1002/prot.26655","DOIUrl":"10.1002/prot.26655","url":null,"abstract":"Bacterial ribosomes require three initiation factors IF1, IF2, and IF3 during the initial steps of translation. These IFs ensure correct base pairing of the initiator tRNA anticodon with the start codon in the mRNA located at the P-site of the 30S ribosomal subunit. IF3 is one of the first IFs to bind to the 30S and plays a crucial role in the selection of the correct start codon and codon: anticodon base pairing. IF3 also prevents the premature association of the 50S subunit of ribosomes and aids in ribosome recycling. IF3 is reported to change binding sites and conformation to ensure translation initiation fidelity. A recent study suggested an initial binding of IF3 CTD away from the P-site and that IF1 and IF2 promote the movement of CTD to the P-site and concomitant movement of NTD. Hence, to visualize the position of IF3 in the absence of any other IFs, we determined cryo-EM structure of the 30S-IF3 complex. The map shows that IF3 is present in an extended conformation with CTD present at the P-site and NTD near the platform even in the absence of IF1 and IF2. Hence, IF3 CTD binds at the P-site and moves away during the accommodation of the initiator tRNA at the P-site in the later steps of translation initiation. Overall, we report the structure of 30S-IF3 which demystifies the starting binding site and conformation of IF3 on the 30S ribosomal subunit.","PeriodicalId":56271,"journal":{"name":"Proteins-Structure Function and Bioinformatics","volume":" ","pages":"279-286"},"PeriodicalIF":3.2,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139041000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0