发布求助
文献互助 智能选刊 最新文献

Structure最新文献

筛选
英文 中文
Structural basis of human uromodulin filament networks in uropathogen capture 人尿调蛋白丝网在尿路病原体捕获中的结构基础
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-08 DOI: 10.1016/j.str.2025.04.011
Andrew N. Chang, Gabriele Cerutti, Yuki Ogawa, Alia Basler, Willa Switzer, Mia Eng-Kohn, Carolyn Lee, Anthony W.P. Fitzpatrick
{"title":"Structural basis of human uromodulin filament networks in uropathogen capture","authors":"Andrew N. Chang, Gabriele Cerutti, Yuki Ogawa, Alia Basler, Willa Switzer, Mia Eng-Kohn, Carolyn Lee, Anthony W.P. Fitzpatrick","doi":"10.1016/j.str.2025.04.011","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.011","url":null,"abstract":"Uromodulin (UMOD), the most abundant protein in human urine, is essential for kidney function and urinary tract health. UMOD forms filaments that bind to uropathogenic bacteria, facilitating their aggregation and clearance from the urinary tract. Here, we present the cryo-electron microscopy (cryo-EM) structure of the bacteria-binding D10C domain of UMOD and reveal its binding to the filament core. The details of D10C-core binding explain the formation of distinct filament lattice architectures adopted by UMOD. The D10C-core binding interface gives rise to diverse filament lattice structures, ranging from open and expansive to compact and dense conformations, or a combination of both. We hypothesize that other molecules present in urine may act as cross-linking agents, further stabilizing this binding interface and facilitating the connection of individual filaments into larger networks capable of effectively trapping bacteria. Structural mapping of kidney disease-related mutations points toward the abolition of disulfide bonds and promotion of mutant UMOD aggregation.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"8 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143920768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
The YEATS domain is a selective reader of histone methacrylation YEATS结构域是组蛋白甲基化的选择性读卡器
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-07 DOI: 10.1016/j.str.2025.04.010
Dustin C. Becht, Jiabao Song, Karthik Selvam, Kejun Yin, Weizhi Bai, Yingming Zhao, Ronghu Wu, Y. George Zheng, Tatiana G. Kutateladze
{"title":"The YEATS domain is a selective reader of histone methacrylation","authors":"Dustin C. Becht, Jiabao Song, Karthik Selvam, Kejun Yin, Weizhi Bai, Yingming Zhao, Ronghu Wu, Y. George Zheng, Tatiana G. Kutateladze","doi":"10.1016/j.str.2025.04.010","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.010","url":null,"abstract":"Metabolically regulated lysine acylation modifications in proteins play a major role in epigenetic processes and cellular homeostasis. A new type of histone acylation, lysine methacrylation, has recently been identified but remains poorly characterized. Here, we show that lysine methacrylation can be generated through metabolism of sodium methacrylate and enzymatically removed in cells, and that the YEATS domain but not bromodomain recognizes this modification. Structural and biochemical analyses reveal the π-π-π-stacking mechanism for binding of the YEATS domain of ENL to methacrylated histone H3K18 (H3K18mc). Using mass spectrometry proteomics, we demonstrate that methacrylate induces global methacrylation of a set of proteins that differs from the set of methacrylated proteins associated with valine metabolism. These findings suggest that high levels of methacrylate may potentially perturb cellular functions of these proteins by altering protein methacrylation profiles.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"31 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143915676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Asymmetric structure of podophage N4 from the Schitoviridae family reveals a type of tube-sheath short-tail architecture Schitoviridae家族的足噬体N4的不对称结构揭示了一种管鞘短尾结构
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-02 DOI: 10.1016/j.str.2025.04.008
Jing Zheng, Hao Pang, Hao Xiao, Junquan Zhou, Zhonghua Liu, Wenyuan Chen, Hongrong Liu
{"title":"Asymmetric structure of podophage N4 from the Schitoviridae family reveals a type of tube-sheath short-tail architecture","authors":"Jing Zheng, Hao Pang, Hao Xiao, Junquan Zhou, Zhonghua Liu, Wenyuan Chen, Hongrong Liu","doi":"10.1016/j.str.2025.04.008","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.008","url":null,"abstract":"The tails of the majority of reported podophages are typically composed of an adaptor, a nozzle, and a needle, and flanked by six or twelve fibers. However, the <em>Schitoviridae</em> family, as represented by podophage N4, exhibits a different tail architecture that remains poorly understood. In this study, we employed cryoelectron microscopy (cryo-EM) to determine the atomic structures of mature and empty podophage N4 particles. The N4 tail, which is connected to the head by a portal and flanked by 12 fibers, comprises an adaptor, a 12-fold extended tail tube encircled by a 6-fold tail sheath, and a plug. The extended tail sheath is composed of two proteins, gp65 and gp64. Furthermore, we identified two distinct tail conformations in the mature podophage N4. Our structures provide insights into the mechanisms of ejection and early transcription of podophage N4, as well as for N4-like phages and CrAssphages.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"2 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143897519","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Introducing Bonnie Murphy, Ville Kaila, Maxie Roessler, Volha Chukhutsina, Alisia Fadini, Sonya Hanson, Filipe Maia, and Kirill Kovalev 有请Bonnie Murphy， Ville Kaila, Maxie Roessler, Volha Chukhutsina, alicia Fadini, Sonya Hanson， Filipe Maia和Kirill Kovalev
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.003
Bonnie J. Murphy, Ville R.I. Kaila, Maxie M. Roessler, Volha Chukhutsina, Alisia Fadini, Sonya M. Hanson, Filipe R.N.C. Maia, Kirill Kovalev
{"title":"Introducing Bonnie Murphy, Ville Kaila, Maxie Roessler, Volha Chukhutsina, Alisia Fadini, Sonya Hanson, Filipe Maia, and Kirill Kovalev","authors":"Bonnie J. Murphy, Ville R.I. Kaila, Maxie M. Roessler, Volha Chukhutsina, Alisia Fadini, Sonya M. Hanson, Filipe R.N.C. Maia, Kirill Kovalev","doi":"10.1016/j.str.2025.04.003","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.003","url":null,"abstract":"In this Voices article, we introduce eight impressive scientists at different career stages who spoke at the recent “8th Ringberg Workshop on Structural Biology (with FELs)” organized by Ilme Schlichting from the Max Planck Institute for Medical Research, Heidelberg. We asked the authors to tell us more about themselves and their exciting research.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"44 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Putting the brakes on endocytosis 抑制内吞作用
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.001
Bernard T. Kelly
{"title":"Putting the brakes on endocytosis","authors":"Bernard T. Kelly","doi":"10.1016/j.str.2025.04.001","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.001","url":null,"abstract":"In this issue of <em>Structure</em>, Horatscheck et al.<span><span><sup>1</sup></span></span> report the isolation and characterization of two improved small molecule drugs for the selective inhibition of clathrin-mediated endocytosis.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"71 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Cryo-ET unravels the mystery of Ad5-nCoV vaccines Cryo-ET揭开了Ad5-nCoV疫苗的神秘面纱
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.006
Chang Liu, Zunlong Ke
{"title":"Cryo-ET unravels the mystery of Ad5-nCoV vaccines","authors":"Chang Liu, Zunlong Ke","doi":"10.1016/j.str.2025.04.006","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.006","url":null,"abstract":"The Ad5-nCoV vaccine (Convidecia) against COVID-19 showed promising clinical results. However, the molecular mechanisms underlying its high immunogenicity and potential adverse reactions have remained elusive. In this issue of <em>Structure</em>, Dong et al.<span><span><sup>1</sup></span></span> employed cryo-electron tomography as a powerful technique to show that abundant prefusion spike protein formation is induced by Ad5-nCoV vaccines.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"12 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Functional conformations or poor mimetics? 功能构象还是拙劣的模仿者？
IF 5.7 2区 生物学
Structure Pub Date : 2025-05-01 DOI: 10.1016/j.str.2025.04.002
Hugues Nury, Rouslan G. Efremov
{"title":"Functional conformations or poor mimetics?","authors":"Hugues Nury, Rouslan G. Efremov","doi":"10.1016/j.str.2025.04.002","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.002","url":null,"abstract":"Membrane proteins function within lipid membranes but require mimetics for structural studies. In this issue of <em>Structure</em>, Hoffmann et al.<span><span><sup>1</sup></span></span> show how different mimetics bias the conformational spectrum of the MsbA transporter. This study highlights the need for improved membrane mimetics and sustained efforts to link conformations to function.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"45 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143893157","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
A distinctive IGHV3-66 SARS-CoV-2 neutralizing antibody elicited by primary infection with an Omicron variant 一种独特的IGHV3-66 SARS-CoV-2中和抗体由原代感染引起
IF 5.7 2区 生物学
Structure Pub Date : 2025-04-29 DOI: 10.1016/j.str.2025.04.005
Qing Fan, Congcong Liu, Huimin Guo, Shilong Tang, Haiyan Wang, Bing Zhou, Yuehong Sun, Miao Wang, Xiangyang Ge, Lei Liu, Bin Ju, Zheng Zhang
{"title":"A distinctive IGHV3-66 SARS-CoV-2 neutralizing antibody elicited by primary infection with an Omicron variant","authors":"Qing Fan, Congcong Liu, Huimin Guo, Shilong Tang, Haiyan Wang, Bing Zhou, Yuehong Sun, Miao Wang, Xiangyang Ge, Lei Liu, Bin Ju, Zheng Zhang","doi":"10.1016/j.str.2025.04.005","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.005","url":null,"abstract":"SARS-CoV-2 Omicron sub-variants continuously evolve under the pressure of neutralizing antibodies (nAbs), eliminating numerous potential elite monoclonal nAbs. The IGHV3-53/3-66 public nAbs have great potential for neutralizing SARS-CoV-2. However, it has been unclear whether a primary Omicron infection could also induce IGHV3-53/3-66 nAbs. In this study, we report an IGHV3-66-encoding monoclonal nAb, ConBA-998, that was elicited by primary infection with BA.1. ConBA-998 is an Omicron-dependent nAb with high binding affinity that triggers the shedding of the S1 subunit from the spike protein. The cryo-electron microscopy (cryo-EM) structure revealed the interactions between ConBA-998 and the Omicron BA.1 spike protein. ConBA-998 has a distinctive binding mode to receptor-binding domain (RBD) that differs from canonical IGHV3-53/3-66 nAbs. Overall, our findings indicate that Omicron may elicit unique specific nAbs distinct from those induced by pre-Omicron variants, providing further insights into SARS-CoV-2 variant-specific antibody responses.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"37 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143884937","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Structural insights into the receptor-binding domain of bat coronavirus ZXC21 蝙蝠冠状病毒ZXC21受体结合域的结构分析
IF 5.7 2区 生物学
Structure Pub Date : 2025-04-29 DOI: 10.1016/j.str.2025.04.004
Chenghai Wang, Xiaoyan Nan, Yang Deng, Shilong Fan, Xin Li, Jun Lan
{"title":"Structural insights into the receptor-binding domain of bat coronavirus ZXC21","authors":"Chenghai Wang, Xiaoyan Nan, Yang Deng, Shilong Fan, Xin Li, Jun Lan","doi":"10.1016/j.str.2025.04.004","DOIUrl":"https://doi.org/10.1016/j.str.2025.04.004","url":null,"abstract":"Bat coronaviruses ZXC21 and ZC45 were discovered before the COVID-19 outbreak and share approximately 86% genome homology with SARS-CoV-2. Earlier studies indicated that ZXC21 and ZC45 may be involved in the emergence of SARS-CoV-2. However, the cell invasion mechanisms of ZXC21 and ZC45 remain unclear. Here, we determined the crystal structure of the ZXC21 receptor-binding domain (RBD) and found that the core structure shared high similarity with SARS-CoV-2, MERS-CoV, human coronavirus (HCoV)-HKU1, SARS-CoV, and HCoV-OC43 RBDs, whereas the receptor-binding motifs (RBMs) differ. We demonstrated that the ZXC21 RBD had no interaction with the human coronavirus receptors angiotensin-converting enzyme 2 (ACE2), dipeptidylpeptidase 4 (DPP4), aminopeptidase N (APN), or transmembrane serine protease 2 (TMPRSS2) by surface plasmon resonance (SPR). Moreover, the P5S-3B11 Fab can bind to the ZXC21 RBD, indicating that this SARS-CoV-2 core-targeting antibody may retain neutralizing activity toward the ZXC21 coronavirus. Our results revealed the bat coronavirus ZXC21 RBD structure, which may provide further insights into the evolution of SARS-CoV-2 and the other human beta-coronaviruses.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"18 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143884936","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
Cholesterol-dependent dimerization and conformational dynamics of EphA2 receptors from coarse-grained and all-atom simulations 来自粗粒度和全原子模拟的EphA2受体的胆固醇依赖性二聚化和构象动力学
IF 5.7 2区 生物学
Structure Pub Date : 2025-04-24 DOI: 10.1016/j.str.2025.03.014
Amita Rani Sahoo, Nisha Bhattarai, Matthias Buck
{"title":"Cholesterol-dependent dimerization and conformational dynamics of EphA2 receptors from coarse-grained and all-atom simulations","authors":"Amita Rani Sahoo, Nisha Bhattarai, Matthias Buck","doi":"10.1016/j.str.2025.03.014","DOIUrl":"https://doi.org/10.1016/j.str.2025.03.014","url":null,"abstract":"The EphA2 transmembrane receptor regulates cellular growth, differentiation, and motility, and its overexpression in various cancers makes it a potential biomarker for clinical cancer management. EphA2 signaling occurs through ligand-induced dimerization where the transmembrane (TM) and juxtamembrane (JM) domains play crucial roles in stabilizing the dimer conformations, thereby facilitating signal transduction. Electrostatic interactions between basic JM residues and signaling lipids (PIP2 and PIP3) regulate phosphorylation while cholesterol’s potential role in modulating EphA2 activation remains unclear. To investigate this, we modeled the TM-full JM peptide of EphA2 and employed coarse-grain and all-atom simulations to investigate its dimerization in cholesterol-rich and cholesterol-deficient membranes. Our findings reveal that cholesterol stabilizes specific TM dimers and TM-JM interactions with PIP2, highlighting the importance of membrane composition in EphA2 dimerization, oligomerization, and clustering. These insights enhance our understanding of lipid-mediated regulation of EphA2 and its implications in receptor signaling and cancer progression.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"44 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143867002","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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
首页 上一页
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整，为了账户安全，请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们：info@booksci.cn Book学术提供免费学术资源搜索服务，方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号：604180095
Book学术官方微信