Biomolecular NMR Assignments最新文献_第4页

Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime 快速 MAS 机制下 α-突触核蛋白淀粉样纤维的固态 NMR 主干化学位移分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-29 DOI: 10.1007/s12104-024-10186-2

Zigmantas Toleikis, Piotr Paluch, Ewelina Kuc, Jana Petkus, Darius Sulskis, Mai-Liis Org-Tago, Ago Samoson, Vytautas Smirnovas, Jan Stanek, Alons Lends

引用次数: 0

Backbone and methyl side-chain resonance assignments of the Fab fragment of adalimumab 阿达木单抗 Fab 片段的骨架和甲基侧链共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-26 DOI: 10.1007/s12104-024-10187-1

Muzaddid Sarker, Yves Aubin

引用次数: 0

Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles 拉沙病毒跨膜结构域在洗涤剂胶束中的融合前和融合后状态的分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-25 DOI: 10.1007/s12104-024-10184-4

Patrick M. Keating, Jinwoo Lee

{"title":"Assignment of the Lassa virus transmembrane domain in the prefusion and postfusion states in detergent micelles","authors":"Patrick M. Keating, Jinwoo Lee","doi":"10.1007/s12104-024-10184-4","DOIUrl":"10.1007/s12104-024-10184-4","url":null,"abstract":"<div><p>Lassa virus (LASV) is the most prevalent member of the arenavirus family and the causative agent of Lassa fever, a viral hemorrhagic fever. Although there are annual outbreaks in West Africa, and recently isolated cases worldwide, there are no current therapeutics or vaccines. As such, LASV poses a significant global public health threat. One of the key steps in LASV infection is delivering its genetic material by fusing its viral membrane with the host cell membrane. This process is facilitated by significant conformational changes within glycoprotein 2 (GP2), yielding distinct prefusion and postfusion structural states. However, structural information is missing to understand the changes that occur in the transmembrane domain (TM) during the fusion process. Previously, we showed that the TM undergoes pH-dependent structural changes that result in a helical extension. Here, we provide the <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C assignment of the LASV TM backbone in the prefusion and postfusion states. We also provide the <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C assignment of two mutants, G429P and D432P, which prevent this helical extension. These results will help understand the role the TM plays in membrane fusion and can lead to the design of therapeutics against LASV infection.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"165 - 169"},"PeriodicalIF":0.8,"publicationDate":"2024-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141445096","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

NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes 多细胞细菌信号体中细胞死亡执行结构域 BELL2 的核磁共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-22 DOI: 10.1007/s12104-024-10183-5

Loic Delcourte, Corinne Sanchez, Estelle Morvan, Mélanie Berbon, Axelle Grélard, Claire Saragaglia, Thierry Dakhli, Stéphane Thore, Benjamin Bardiaux, Birgit Habenstein, Brice Kauffmann, Sven J. Saupe, Antoine Loquet

{"title":"NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes","authors":"Loic Delcourte, Corinne Sanchez, Estelle Morvan, Mélanie Berbon, Axelle Grélard, Claire Saragaglia, Thierry Dakhli, Stéphane Thore, Benjamin Bardiaux, Birgit Habenstein, Brice Kauffmann, Sven J. Saupe, Antoine Loquet","doi":"10.1007/s12104-024-10183-5","DOIUrl":"10.1007/s12104-024-10183-5","url":null,"abstract":"<div><p>Signalosomes are high-order protein machineries involved in complex mechanisms controlling regulated immune defense and cell death execution. The immune response is initiated by the recognition of exogeneous or endogenous signals, triggering the signalosome assembly process. The final step of signalosome fate often involves membrane-targeting and activation of pore-forming execution domains, leading to membrane disruption and ultimately cell death. Such cell death-inducing domains have been thoroughly characterized in plants, mammals and fungi, notably for the fungal cell death execution protein domain HeLo. However, little is known on the mechanisms of signalosome-based immune response in bacteria, and the conformation of cell death executors in bacterial signalosomes is still poorly characterized. We recently uncovered the existence of NLR signalosomes in various multicellular bacteria and used genome mining approaches to identify putative cell death executors in <i>Streptomyces olivochromogenes</i>. These proteins contain a C-terminal amyloid domain involved in signal transmission and a N-terminal domain, termed BELL for Bacteria analogous to fungal HeLL (HeLo-like), presumably responsible for membrane-targeting, pore-forming and cell death execution. In the present study, we report the high yield expression of <i>S. olivochromogenes</i> BELL2 and its characterization by solution NMR spectroscopy. BELL is folded in solution and we report backbone and sidechain assignments. We identified five α-helical secondary structure elements and a folded core much smaller than its fungal homolog HeLo. This study constitutes the first step toward the NMR investigation of the full-length protein assembly and its membrane targeting.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"159 - 164"},"PeriodicalIF":0.8,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141439906","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

Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19 人类副病毒病原体 B19 的 VP1u N 端受体结合域的骨架核磁共振共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-21 DOI: 10.1007/s12104-024-10181-7

Maria Luiza Caldas Nogueira, Renuk Lakshmanan, Gwladys Rivière, Mario Mietzsch, Antonette Bennett, Robert McKenna, Joanna R. Long

{"title":"Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19","authors":"Maria Luiza Caldas Nogueira, Renuk Lakshmanan, Gwladys Rivière, Mario Mietzsch, Antonette Bennett, Robert McKenna, Joanna R. Long","doi":"10.1007/s12104-024-10181-7","DOIUrl":"10.1007/s12104-024-10181-7","url":null,"abstract":"<div><p>Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA<sub>2</sub>) domain, crucial for endosomal escape during cellular trafficking. Both domains are indispensable for infection, making the RBD a plausible drug target for inhibitors against B19V, as it is located on the exterior surface of the virus. To date, no experimental structural information has been available for the VP1u component for any Parvovirus. Here we report the backbone NMR resonance assignments for the RBD of B19V and demonstrate it forms a stable structure. The backbone chemical shifts are in good agreement with a structure predicted by AlphaFold, validating that the RBD contains three helices connected by tight turns. This RBD construct can now be used for further NMR studies, including assignment of full-length VP1u, determination of protein-protein interaction interfaces, and development of B19 antivirals specific to the RBD domain.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"147 - 152"},"PeriodicalIF":0.8,"publicationDate":"2024-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141431063","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

1H, 13C and 15N backbone resonance assignment of Cel45A from Phanerochaete chrysosporium 来自 Phanerochaete chrysosporium 的 Cel45A 的 1H、13C 和 15N 主干共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-18 DOI: 10.1007/s12104-024-10182-6

Laura Okmane, Mats Sandgren, Jerry Ståhlberg, Gustav Nestor

引用次数: 0

Backbone triple resonance assignments of the dimerization domain of NF-kappaB p52 subunit NF-kappaB p52 亚基二聚化结构域的骨架三重共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-10 DOI: 10.1007/s12104-024-10179-1

Sunirmala Sahoo, Nitin Dhaka, Sulakshana P. Mukherjee

引用次数: 0

Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1 细胞色素 MtoD 的共振赋值来自于纤毛虫 ES-1 的细胞外电子摄取途径。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-07 DOI: 10.1007/s12104-024-10180-8

Anaísa Coelho, José M. Silva, Francesca Cantini, Mario Piccioli, Ricardo O. Louro, Catarina M. Paquete

{"title":"Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1","authors":"Anaísa Coelho, José M. Silva, Francesca Cantini, Mario Piccioli, Ricardo O. Louro, Catarina M. Paquete","doi":"10.1007/s12104-024-10180-8","DOIUrl":"10.1007/s12104-024-10180-8","url":null,"abstract":"<div><p>The contribution of Fe(II)-oxidizing bacteria to iron cycling in freshwater, groundwater, and marine environments has been widely recognized in recent years. These organisms perform extracellular electron transfer (EET), which constitutes the foundations of bioelectrochemical systems for the production of biofuels and bioenergy. It was proposed that the Gram-negative bacterium <i>Sideroxydans lithotrophicus</i> ES-1 oxidizes soluble ferrous Fe(II) at the surface of the cell and performs EET through the Mto redox pathway. This pathway is composed by the periplasmic monoheme cytochrome MtoD that is proposed to bridge electron transfer between the cell exterior and the cytoplasm. This makes its functional and structural characterization, as well as evaluating the interaction process with its physiological partners, essential for understanding the mechanisms underlying EET. Here, we report the complete assignment of the heme proton and carbon signals together with a near-complete assignment of <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone and side chain resonances for the reduced, diamagnetic form of the protein. These data pave the way to identify and structurally map the molecular interaction regions between the cytochrome MtoD and its physiological redox partners, to explore the EET processes of <i>S. lithotrophicus</i> ES-1.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"139 - 146"},"PeriodicalIF":0.8,"publicationDate":"2024-06-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511738/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141282649","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

NMR chemical shift assignment of Drosophila odorant binding protein 44a in complex with 8(Z)-eicosenoic acid 果蝇气味结合蛋白 44a 与 8(Z)-eicosenoic acid 复合物的核磁共振化学位移分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-06-01 DOI: 10.1007/s12104-024-10178-2

Myriam L. Cotten, Mary R. Starich, Yi He, Jun Yin, Quan Yuan, Nico Tjandra

{"title":"NMR chemical shift assignment of Drosophila odorant binding protein 44a in complex with 8(Z)-eicosenoic acid","authors":"Myriam L. Cotten, Mary R. Starich, Yi He, Jun Yin, Quan Yuan, Nico Tjandra","doi":"10.1007/s12104-024-10178-2","DOIUrl":"10.1007/s12104-024-10178-2","url":null,"abstract":"<div><p>The odorant binding protein, OBP44a is one of the most abundant proteins expressed in the brain of the developing fruit fly <i>Drosophila melanogaster</i>. Its cellular function has not yet been determined. The OBP family of proteins is well established to recognize hydrophobic molecules. In this study, NMR is employed to structurally characterize OBP44a. NMR chemical shift perturbation measurements confirm that OBP44a binds to fatty acids. Complete assignments of the backbone chemical shifts and secondary chemical shift analysis demonstrate that the apo state of OBP44a is comprised of six α-helices. Upon binding 8(Z)-eicosenoic acid (8(Z)-C20:1), the OBP44a C-terminal region undergoes a conformational change, from unstructured to α-helical. In addition to C-terminal restructuring upon ligand binding, some hydrophobic residues show dramatic chemical shift changes. Surprisingly, several charged residues are also strongly affected by lipid binding. Some of these residues could represent key structural features that OBP44a relies on to perform its cellular function. The NMR chemical shift assignment is the first step towards characterizing the structure of OBP44a and how specific residues might play a role in lipid binding and release. This information will be important in deciphering the biological function of OBP44a during fly brain development.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"129 - 134"},"PeriodicalIF":0.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11511771/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141185868","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

Backbone and methyl side-chain resonance assignments of the single chain Fab fragment of trastuzumab 曲妥珠单抗单链 Fab 片段的骨架和甲基侧链共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-05-08 DOI: 10.1007/s12104-024-10177-3

Donald Gagné, James M. Aramini, Yves Aubin

引用次数: 0