[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-450420-105":59,"doc-detail-450420-en":130},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":123,"head_meta":125,"extra_data":127,"updated_unix":129},105,"en","structural-analysis-of-a-motor-with-increased-mechanical-output-reveals-new-transitions-in-kinesin-microtubule-motility-research-findings","Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility - research findings","","Kinesin motors use ATP to generate cellular force, but the structural changes driving force production remain unclear. This study reports structural and mechanistic insights into a minus-end-directed kinesin-14 variant with increased mechanical output: tighter microtubule binding and faster velocity than wild type. High-resolution structures and molecular dynamics identify new nucleotide hydrolysis transitions, coupling ADP release to central β-sheet twisting and stalk stabilization, then ATP binding-driven fluctuations and recovery-state β-sheet melting that facilitate Pi release. The central β-sheet is proposed as the elastic spring element enabling force, with broader implications for kinesins.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/structural-analysis-of-a-motor-with-increased-mechanical-output-reveals-new-transitions-in-kinesin-microtubule-motility-research-findings/450420/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/structural-analysis-of-a-motor-with-increased-mechanical-output-reveals-new-transitions-in-kinesin-microtubule-motility-research-findings/450420.png","ImageObject",300,407,{"name":92,"@type":93},"\tCallum ","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-05","2026-09-30",true,{"@type":102,"interactionType":103,"userInteractionCount":81},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What kinesin variant is studied, and what mechanical improvement is observed?","Question",{"text":112,"@type":113},"A minus-end-directed kinesin-14 variant is examined. It shows increased mechanical output, including tighter microtubule binding and faster velocity than the wild type.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"What new transitions are revealed during the nucleotide hydrolysis cycle?",{"text":117,"@type":113},"High-resolution structures and molecular dynamics uncover previously unobserved transitions. ADP release triggered by microtubule binding couples to central β-sheet twisting and stalk stabilization, and later ATP binding drives stalk fluctuations and neck-mimic swinging.",{"name":119,"@type":110,"acceptedAnswer":120},"How do the power stroke and recovery stroke differ, and what role does the β-sheet play?",{"text":121,"@type":113},"The power stroke involves large stalk rotation followed by motor detachment from microtubules. The recovery stroke occurs while bound to ADP with free Pi, with β-strand-to-loop transitions or β-sheet melting that supports Pi release, indicating the central β-sheet functions as the elastic spring for force production.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},450420,1790772521,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":39,"category_name":40,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":81,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":139,"language":140,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":67,"update_tm":144,"read_time":145},137451211410,"https://ap-avatar.wpscdn.com/avatar/2000bb0a9246f588df?x-image-process=image/resize,m_fixed,w_180,h_180&k=1786362646172706240","[www. nature.com/scientificreports](www. nature.com/scientificreports)  \nOPEN  \nStructural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility  \nSatoki Shibata1,9, Matthew Y. Wang2,9, Tsuyoshi Imasaki1,9􀀍, Hideki Shigematsu3, Diego Ugarte La Torre4, Yuanyuan Wei5, Chacko Jobichen6,8, Hajime Hagio1, J. Sivaraman6, Yuji Sugita4,7, SharynA. Endow2,5􀀍 & Ryo Nitta1􀀍  \nKinesin motors use ATP to produce force in cells, yet the conformational changes that generate force remain uncertain. Here, we report structural and mechanistic insights into a minus-end-directed kinesin-14 that exhibits increased mechanical output – the variant motor binds microtubules more tightly and moves with faster velocity than wild type. High-resolution structures, together with molecular dynamics simulations, reveal previously unobserved transitions in the nucleotide hydrolysis cycle. ADP release, triggered by microtubule binding, is coupled to twisting of the central β-sheet and stabilization of the stalk prior to the power stroke. ATP binding induces stalk fluctuations and a swing of the neck mimic, an element analogous to the kinesin-1 neck linker, resembling neck linker docking in plus-end-directed kinesins. The power stroke, characterized by a large stalk rotation, is followed by motor detachment from microtubules. The subsequent recovery stroke occurs while the motor is bound toADP and free Pi, accompanied by β-strand-to-loop transitions, or β-sheet melting, implying that β-sheet refolding facilitates Pi release. The observed twisting and melting identify the central β -sheet as the long-sought elastic element or spring required for motor force production. The transitions we observe in kinesin-14 may also apply to other kinesins – this remains to be tested.  \nKeywords Motor force production, Power stroke fluctuations, Neck mimic docking, ADP + free Pi state, Beta-sheet distortion, Motor spring-like element  \nMotor proteins – the dyneins, myosins, and kinesins – hydrolyze ATP and bind to microtubules or actin filaments, producing force and steps along their filament, or sliding of filaments relative to one another. The mechanism by which motor proteins produce force and movement is still not fully understood. The motor force-generating mechanism is known to rely on ATP binding, hydrolysis, and release of hydrolysis products, coupled to filament binding and release1. This has led to the idea that motility is regulated by the nucleotide state of the motor, together with motor-filament interactions2,3. Motors have been hypothesized to contain a springlike or elastic element that compresses in a specific nucleotide state, storing free energy, and then releases in a subsequent state, producing force1, but the spring has not yet been definitively identified. The movements in the motor domain due to nucleotide binding, hydrolysis, and product release are small, based on kinetic studies of myosin4, a motor evolutionarily related to the kinesin family5, and other ATP-binding enzymes6. This has also been observed in structural studies of myosin in different nucleotide states3,7.  \n1Division of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, 650-0017 Kobe, Japan. 2Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. 3Structural Biology Division, Synchrotron Radiation Research Institute, SPring-8, Sayo, Hyogo 679-5184, Japan. 4Computational Biophysics Research Team, RIKEN Center for Computational Science, 650-0047 Kobe, Japan. 5Neuroscience & Behavioral Disorders Programme, Duke-NUS School of Medicine, 169857 Singapore, Singapore. 6Department of Biological Sciences, National University of Singapore, 117558 Singapore, Singapore. 7Theoretical Molecular Science Laboratory, RIKEN Pioneering Research Institute, Saitama 351-0198, Japan. 8Present address: School of Chemistry and Molecular Bioscience, University of ","cbCainDxRBtetLBA","https://ap.wps.com/l/cbCainDxRBtetLBA","pdf",6911862,21,"English","# Structural and mechanistic overview\n## Increased mechanical output of kinesin-14 variant\n## New transitions in the nucleotide hydrolysis cycle\n# Coupling of nucleotide states to conformational changes\n## ADP release and central β-sheet twisting\n## ATP binding, neck-mimic docking, and power stroke\n# Detachment and recovery strokes\n## β-sheet melting and Pi release\n## Central β-sheet as the spring element\n# Comparison with kinesin-1 and kinesin-14 mechanisms","[{\"question\":\"What kinesin variant is studied, and what mechanical improvement is observed?\",\"answer\":\"A minus-end-directed kinesin-14 variant is examined. It shows increased mechanical output, including tighter microtubule binding and faster velocity than the wild type.\"},{\"question\":\"What new transitions are revealed during the nucleotide hydrolysis cycle?\",\"answer\":\"High-resolution structures and molecular dynamics uncover previously unobserved transitions. ADP release triggered by microtubule binding couples to central β-sheet twisting and stalk stabilization, and later ATP binding drives stalk fluctuations and neck-mimic swinging.\"},{\"question\":\"How do the power stroke and recovery stroke differ, and what role does the β-sheet play?\",\"answer\":\"The power stroke involves large stalk rotation followed by motor detachment from microtubules. The recovery stroke occurs while bound to ADP with free Pi, with β-strand-to-loop transitions or β-sheet melting that supports Pi release, indicating the central β-sheet functions as the elastic spring for force production.\"}]","Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility - research findings | PDF",1790733171,53]