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Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 Å resolution. A comparison with vertebrate F-actin 酵母adp -肌动蛋白丝在2.5 Å分辨率下的低温电镜重建。与脊椎动物f -肌动蛋白的比较
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-10 DOI: 10.1016/j.str.2024.12.008
Sarah R. Stevenson, Svetomir B. Tzokov, Indrajit Lahiri, Kathryn R. Ayscough, Per A. Bullough
{"title":"Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 Å resolution. A comparison with vertebrate F-actin","authors":"Sarah R. Stevenson, Svetomir B. Tzokov, Indrajit Lahiri, Kathryn R. Ayscough, Per A. Bullough","doi":"10.1016/j.str.2024.12.008","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.008","url":null,"abstract":"The core component of the actin cytoskeleton is the globular protein G-actin, which reversibly polymerizes into filaments (F-actin). Budding yeast possesses a single actin that shares 87%–89% sequence identity with vertebrate actin isoforms. Previous structural studies indicate very close overlap of main-chain backbones. Intriguingly, however, substitution of yeast <em>ACT1</em> with vertebrate β-cytoplasmic actin severely disrupts cell function and the substitution with a skeletal muscle isoform is lethal. Here we report a 2.5 Å structure of budding yeast F-actin. Previously unresolved side-chain information allows us to highlight four main differences in the comparison of yeast and vertebrate ADP F-actins: a more open nucleotide binding pocket; a more solvent exposed C-terminus; a rearrangement of inter-subunit binding interactions in the vicinity of the D loop and changes in the hydrogen bonding network in the vicinity of histidine 73 (yeast actin) and methyl-histidine 73 (vertebrate actin).","PeriodicalId":22168,"journal":{"name":"Structure","volume":"8 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142939576","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-EM structure and complementary drug efflux activity of the Acinetobacter baumannii multidrug efflux pump AdeG 鲍曼不动杆菌多药外排泵AdeG的低温电镜结构和补充药物外排活性
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-10 DOI: 10.1016/j.str.2024.12.009
Zhenlin Ouyang, Wenbo He, Di Wu, Hao An, Lei Duan, Min Jiao, Xiaoyu He, Qinyue Yu, Jiaxin Zhang, Qian Qin, Ruochen Wang, Fang Zheng, Peter M. Hwang, Xiaoting Hua, Li Zhu, Yurong Wen
{"title":"Cryo-EM structure and complementary drug efflux activity of the Acinetobacter baumannii multidrug efflux pump AdeG","authors":"Zhenlin Ouyang, Wenbo He, Di Wu, Hao An, Lei Duan, Min Jiao, Xiaoyu He, Qinyue Yu, Jiaxin Zhang, Qian Qin, Ruochen Wang, Fang Zheng, Peter M. Hwang, Xiaoting Hua, Li Zhu, Yurong Wen","doi":"10.1016/j.str.2024.12.009","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.009","url":null,"abstract":"Multidrug-resistant <em>Acinetobacter baumannii</em> has emerged as one of the most antibiotic-resistant bacterial pathogens associated with nosocomial infection, with its resistance highly depending on multiple multidrug efflux pumps. Here, we report the cryoelectron microscopy (cryo-EM) structure of <em>Acinetobacter</em> drug efflux G (AdeG), the inner membrane component of one of three important resistance-nodulation-cell division (RND) pump family members in <em>A. baumannii</em>, which is involved in drug resistance to chloramphenicol, trimethoprim, ciprofloxacin, and clindamycin. We systematically compare the structures and substrate binding specificities of AdeG, AdeB, and AdeJ multidrug efflux pumps via molecular docking, revealing potential determinants for drug binding. Knockout experiments demonstrate a functional complementarity between AdeABC, AdeFGH, and AdeIJK. Our study provides a structural understanding of <em>A. baumannii</em> multidrug efflux pump AdeG and reveals complementary drug efflux activity between AdeG and other RND efflux pumps, which may promote further rational drug discovery efforts targeting multidrug efflux pumps.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"31 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142939572","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
Cryoelectron microscopy with elemental sensitivity 元素灵敏度低温电子显微镜
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-02 DOI: 10.1016/j.str.2024.12.003
Hannah Ochner, Tanmay A.M. Bharat
{"title":"Cryoelectron microscopy with elemental sensitivity","authors":"Hannah Ochner, Tanmay A.M. Bharat","doi":"10.1016/j.str.2024.12.003","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.003","url":null,"abstract":"In a recent issue of <em>Nature Methods</em>, Pfeil-Gardiner et al. (2024)<span><span><sup>1</sup></span></span> combine electron energy-loss spectroscopy and single-particle cryoelectron microscopy to allow the spatially resolved imaging of the elemental composition of macromolecules.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"92 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142912107","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
4D structural biology—The 9th Murnau Conference on structural biology 4D结构生物学-第九届摩瑙结构生物学会议
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-02 DOI: 10.1016/j.str.2024.11.012
Janosch Hennig, Cristina Paulino
{"title":"4D structural biology—The 9th Murnau Conference on structural biology","authors":"Janosch Hennig, Cristina Paulino","doi":"10.1016/j.str.2024.11.012","DOIUrl":"https://doi.org/10.1016/j.str.2024.11.012","url":null,"abstract":"The data presented at the 9<sup>th</sup> International Murnau Conference on September 18–21, 2024, the largest recurring structural biology meeting in Central Europe, illustrated the thriving state of the structural biology community. This is largely attributed to the ground-breaking developments over the last decade, which were intensely discussed during the meeting.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142912017","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
AI decodes CNNM Na+/Mg2+ exchange 人工智能解码CNNM Na+/Mg2+交换
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-02 DOI: 10.1016/j.str.2024.12.006
Thushara Nethramangalath, Loren W. Runnels
{"title":"AI decodes CNNM Na+/Mg2+ exchange","authors":"Thushara Nethramangalath, Loren W. Runnels","doi":"10.1016/j.str.2024.12.006","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.006","url":null,"abstract":"In this issue of <em>Structure</em>, Ma et al.<span><span><sup>1</sup></span></span> apply the artificial intelligence system AlphaFold2, which was designed to predict three-dimensional protein structures from amino acid sequences with atomic accuracy, to model the conformal dynamics of the prokaryotic TpCorC and human CNNM2 and CNNM4 transporters, providing mechanistic insight into how sodium drives magnesium efflux.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"25 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142912016","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
It takes two to tango: The second membrane-binding site in peripheral proteins 探戈需要两个：外周蛋白的第二个膜结合位点
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-02 DOI: 10.1016/j.str.2024.12.007
Anand Srivastavava
{"title":"It takes two to tango: The second membrane-binding site in peripheral proteins","authors":"Anand Srivastavava","doi":"10.1016/j.str.2024.12.007","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.007","url":null,"abstract":"In this issue of <em>Structure</em>, Soteriou et al.<span><span><sup>1</sup></span></span> use cell biology, <em>in vitro</em> reconstitution approaches, and molecular dynamics (MD) simulations to characterize the membrane association of AKT1. The authors show that the AKT1 pleckstrin homology domain contains two essential and cooperative PI(3,4,5)P<sub>3</sub>-binding sites that enable stable membrane binding of AKT1 in the requisite orientation required for effective downstream signaling.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"66 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142912059","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
Lysozyme revisited 溶菌酶重新审视
IF 5.7 2区 生物学
Structure Pub Date : 2025-01-02 DOI: 10.1016/j.str.2024.12.005
Esko Oksanen
{"title":"Lysozyme revisited","authors":"Esko Oksanen","doi":"10.1016/j.str.2024.12.005","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.005","url":null,"abstract":"Lysozyme is a model system for crystallographers. In this issue of <em>Structure</em>, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"23 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142912102","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 structure and assembly of the hetero-octameric BLOC-one-related complex 异八聚体block - 1相关配合物的结构与组装
IF 5.7 2区 生物学
Structure Pub Date : 2024-12-30 DOI: 10.1016/j.str.2024.12.001
Xuan Ge, Jinqi Ren, Kewei Gu, Weibin Gong, Kang Shen, Wei Feng
{"title":"The structure and assembly of the hetero-octameric BLOC-one-related complex","authors":"Xuan Ge, Jinqi Ren, Kewei Gu, Weibin Gong, Kang Shen, Wei Feng","doi":"10.1016/j.str.2024.12.001","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.001","url":null,"abstract":"BORC (BLOC-one-related complex) is a hetero-octameric complex, consisting of eight coiled-coil proteins (BORCS1–8). BORC controls lysosomal and synaptic vesicle transport and positioning by recruiting ARL8. The structural mechanisms underlying BORC assembly and ARL8 activation remain unclear. Here, we reconstitute and construct the structural model of this hetero-octameric complex. We find that BORC adopts an extended, rod-like structure made of coiled coils. Two hemicomplexes, each containing four subunits, are joined end-to-end to form the holocomplex. Within each hemicomplex, BORCS1/4/6/8 or BORCS2/3/5/7 assembles into similar helical bundles. We further study how BORC is built and discover a hierarchical assembly process in which BORCS1/2/3/5 forms the core scaffold and recruits other subunits. Mutations in the inter-hemicomplex interfaces result in two hemicomplexes. The association of ARL8 may require the proper assembly of BORC and is primarily mediated by BORCS5. These results provide guidance for further understanding of the biology of BORC.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"168 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901712","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
Physicochemical features of subunit interfaces and their role in self-assembly across the ferritin superfamily 亚基界面的物理化学特征及其在铁蛋白超家族自组装中的作用
IF 5.7 2区 生物学
Structure Pub Date : 2024-12-30 DOI: 10.1016/j.str.2024.12.004
, Soumyananda Chakraborti, Sucharita Dey
{"title":"Physicochemical features of subunit interfaces and their role in self-assembly across the ferritin superfamily","authors":", Soumyananda Chakraborti, Sucharita Dey","doi":"10.1016/j.str.2024.12.004","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.004","url":null,"abstract":"Ferritins are ubiquitous and play a critical role in iron homeostasis. They are classified into four main subfamilies: classical, bacterial, bacterioferritin, and Dps. These are characterized by subunits with a four-helical bundle domain and interact through three distinct regions—one antiparallel interface (IntA) and two perpendicular interfaces (IntB and IntC), collectively forming a cage-like structure. Here, we attempt to characterize the variability of these interfaces across subfamilies. We found that IntA is essential for the dimeric unit assembly and is likely to assemble first, followed by the smaller interfaces of IntB and IntC (in any order), which are crucial for cage formation. These interfaces are unique in that they are less packed, although chemically stable, and their size lies between that of protein-protein complex and obligate homodimers. This study provides a detailed exploration of the ferritin interfaces, offering insights into their assembly and their importance as carrier proteins.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"65 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901713","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 biochemical mechanism of the E2/E3 hybrid enzyme UBE2O 从结构上揭示 E2/E3 混合酶 UBE2O 的生化机制
IF 5.7 2区 生物学
Structure Pub Date : 2024-12-30 DOI: 10.1016/j.str.2024.12.002
Hao Huang, Wenning Zhu, Bin Huang, Ziyang Fu, Yuxian Xiong, Dan Cao, Yuxin Ye, Qing Chang, Wenqi Li, Long Li, Huan Zhou, Xiaogang Niu, Wei Zhang
{"title":"Structural insights into the biochemical mechanism of the E2/E3 hybrid enzyme UBE2O","authors":"Hao Huang, Wenning Zhu, Bin Huang, Ziyang Fu, Yuxian Xiong, Dan Cao, Yuxin Ye, Qing Chang, Wenqi Li, Long Li, Huan Zhou, Xiaogang Niu, Wei Zhang","doi":"10.1016/j.str.2024.12.002","DOIUrl":"https://doi.org/10.1016/j.str.2024.12.002","url":null,"abstract":"The E2/E3 hybrid enzyme UBE2O plays important roles in key biological events, but its autoubiquitination mechanism remains largely unclear. In this study, we determined the crystal structures of full-length (FL) UBE2O from <em>Trametes pubescens</em> (tp) and its ubiquitin-conjugating (UBC) domain. The dimeric FL-tpUBE2O structure revealed interdomain interactions between the conserved regions (CR1-CR2) and UBC. The dimeric intermolecular and canonical ubiquitin/UBC interactions are mechanistically important for UBE2O functions in catalyzing the formation of free polyubiquitin chains and substrate ubiquitination. Beyond dimerization, autoubiquitination within the CR1-CR2 domain also regulates tpUBE2O activity. Additionally, we show that tpUBE2O catalyzes the formation of all seven types of polyubiquitin chains <em>in vitro</em>. The CR1-CR2/UBC and canonical ubiquitin/UBC interactions are important for the polyubiquitination of AMP-activated protein kinase α2 (AMPKα2) by human UBE2O (hUBE2O), which leads to tumorigenesis. These structural insights lay the groundwork for understanding UBE2O’s mechanisms and developing structure-based therapeutics targeting UBE2O.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"81 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901671","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
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