Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement

Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of molecular biology 2018-07, Vol.430 (14), p.2030-2041
Hauptverfasser: Ren, Jinqi, Zhang, Yong, Wang, Shuang, Huo, Lin, Lou, Jizhong, Feng, Wei
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2041
container_issue 14
container_start_page 2030
container_title Journal of molecular biology
container_volume 430
creator Ren, Jinqi
Zhang, Yong
Wang, Shuang
Huo, Lin
Lou, Jizhong
Feng, Wei
description Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)–NL–NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD–NL–NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3. [Display omitted] •Kinesin-3 NL controls the directionality and processivity but is poorly defined.•Structure of the KIF13B MD–NL–NCNT tandem was determined at 2.0-Å resolution.•Kinesin-3 NL is shorter than the predicted one and is even shorter than kinesin-1 NL.•Kinesin-3 NL interacts weakly with MD due to the shorter N-terminal cover strand.•Short NL and its weak interaction with MD account for kinesin-3 processive movement.
doi_str_mv 10.1016/j.jmb.2018.05.010
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2038273887</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022283618304054</els_id><sourcerecordid>2038273887</sourcerecordid><originalsourceid>FETCH-LOGICAL-c419t-157dbcc6234a21561bf8f01bf58144523dbb418d453ab9283b2b69a6161add393</originalsourceid><addsrcrecordid>eNp9kElPwzAQhS0EgrL8AC4oRy4JXmLXESdUVlEWCThbtjMRLklc7KQS_x5XBY5cZqSZ9570PoSOCS4IJuJsUSw6U1BMZIF5gQneQhOCZZVLweQ2mmBMaU4lE3toP8YFxpizUu6iPVpNOa2EnKDHlyGMdhiDbrNLaF0PenC-z3yTDe-QPYL9yOau_4CwPt2nf3R9zrLGh-w5eAsxuhVkD34FHfTDIdppdBvh6GcfoLfrq9fZbT5_urmbXcxzW5JqyAmf1sZaQVmpKeGCmEY2OE0uSVlyympjSiLrkjNtqtTAUCMqLYgguq5ZxQ7Q6SZ3GfznCHFQnYsW2lb34MeoKGaSTpmU0yQlG6kNPsYAjVoG1-nwpQhWa4xqoRJGtcaoMFcJY_Kc_MSPpoP6z_HLLQnONwJIJVcOgorWQW-hdgHsoGrv_on_Blr8gaE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2038273887</pqid></control><display><type>article</type><title>Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement</title><source>Access via ScienceDirect (Elsevier)</source><creator>Ren, Jinqi ; Zhang, Yong ; Wang, Shuang ; Huo, Lin ; Lou, Jizhong ; Feng, Wei</creator><creatorcontrib>Ren, Jinqi ; Zhang, Yong ; Wang, Shuang ; Huo, Lin ; Lou, Jizhong ; Feng, Wei</creatorcontrib><description>Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)–NL–NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD–NL–NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3. [Display omitted] •Kinesin-3 NL controls the directionality and processivity but is poorly defined.•Structure of the KIF13B MD–NL–NCNT tandem was determined at 2.0-Å resolution.•Kinesin-3 NL is shorter than the predicted one and is even shorter than kinesin-1 NL.•Kinesin-3 NL interacts weakly with MD due to the shorter N-terminal cover strand.•Short NL and its weak interaction with MD account for kinesin-3 processive movement.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2018.05.010</identifier><identifier>PMID: 29752968</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>interaction ; intracellular transport ; molecular dynamics simulation ; molecular motor ; X-ray crystallography</subject><ispartof>Journal of molecular biology, 2018-07, Vol.430 (14), p.2030-2041</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright © 2018 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-157dbcc6234a21561bf8f01bf58144523dbb418d453ab9283b2b69a6161add393</citedby><cites>FETCH-LOGICAL-c419t-157dbcc6234a21561bf8f01bf58144523dbb418d453ab9283b2b69a6161add393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2018.05.010$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29752968$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ren, Jinqi</creatorcontrib><creatorcontrib>Zhang, Yong</creatorcontrib><creatorcontrib>Wang, Shuang</creatorcontrib><creatorcontrib>Huo, Lin</creatorcontrib><creatorcontrib>Lou, Jizhong</creatorcontrib><creatorcontrib>Feng, Wei</creatorcontrib><title>Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)–NL–NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD–NL–NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3. [Display omitted] •Kinesin-3 NL controls the directionality and processivity but is poorly defined.•Structure of the KIF13B MD–NL–NCNT tandem was determined at 2.0-Å resolution.•Kinesin-3 NL is shorter than the predicted one and is even shorter than kinesin-1 NL.•Kinesin-3 NL interacts weakly with MD due to the shorter N-terminal cover strand.•Short NL and its weak interaction with MD account for kinesin-3 processive movement.</description><subject>interaction</subject><subject>intracellular transport</subject><subject>molecular dynamics simulation</subject><subject>molecular motor</subject><subject>X-ray crystallography</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp9kElPwzAQhS0EgrL8AC4oRy4JXmLXESdUVlEWCThbtjMRLklc7KQS_x5XBY5cZqSZ9570PoSOCS4IJuJsUSw6U1BMZIF5gQneQhOCZZVLweQ2mmBMaU4lE3toP8YFxpizUu6iPVpNOa2EnKDHlyGMdhiDbrNLaF0PenC-z3yTDe-QPYL9yOau_4CwPt2nf3R9zrLGh-w5eAsxuhVkD34FHfTDIdppdBvh6GcfoLfrq9fZbT5_urmbXcxzW5JqyAmf1sZaQVmpKeGCmEY2OE0uSVlyympjSiLrkjNtqtTAUCMqLYgguq5ZxQ7Q6SZ3GfznCHFQnYsW2lb34MeoKGaSTpmU0yQlG6kNPsYAjVoG1-nwpQhWa4xqoRJGtcaoMFcJY_Kc_MSPpoP6z_HLLQnONwJIJVcOgorWQW-hdgHsoGrv_on_Blr8gaE</recordid><startdate>20180706</startdate><enddate>20180706</enddate><creator>Ren, Jinqi</creator><creator>Zhang, Yong</creator><creator>Wang, Shuang</creator><creator>Huo, Lin</creator><creator>Lou, Jizhong</creator><creator>Feng, Wei</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20180706</creationdate><title>Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement</title><author>Ren, Jinqi ; Zhang, Yong ; Wang, Shuang ; Huo, Lin ; Lou, Jizhong ; Feng, Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-157dbcc6234a21561bf8f01bf58144523dbb418d453ab9283b2b69a6161add393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>interaction</topic><topic>intracellular transport</topic><topic>molecular dynamics simulation</topic><topic>molecular motor</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ren, Jinqi</creatorcontrib><creatorcontrib>Zhang, Yong</creatorcontrib><creatorcontrib>Wang, Shuang</creatorcontrib><creatorcontrib>Huo, Lin</creatorcontrib><creatorcontrib>Lou, Jizhong</creatorcontrib><creatorcontrib>Feng, Wei</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ren, Jinqi</au><au>Zhang, Yong</au><au>Wang, Shuang</au><au>Huo, Lin</au><au>Lou, Jizhong</au><au>Feng, Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2018-07-06</date><risdate>2018</risdate><volume>430</volume><issue>14</issue><spage>2030</spage><epage>2041</epage><pages>2030-2041</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)–NL–NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD–NL–NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3. [Display omitted] •Kinesin-3 NL controls the directionality and processivity but is poorly defined.•Structure of the KIF13B MD–NL–NCNT tandem was determined at 2.0-Å resolution.•Kinesin-3 NL is shorter than the predicted one and is even shorter than kinesin-1 NL.•Kinesin-3 NL interacts weakly with MD due to the shorter N-terminal cover strand.•Short NL and its weak interaction with MD account for kinesin-3 processive movement.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>29752968</pmid><doi>10.1016/j.jmb.2018.05.010</doi><tpages>12</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0022-2836
ispartof Journal of molecular biology, 2018-07, Vol.430 (14), p.2030-2041
issn 0022-2836
1089-8638
language eng
recordid cdi_proquest_miscellaneous_2038273887
source Access via ScienceDirect (Elsevier)
subjects interaction
intracellular transport
molecular dynamics simulation
molecular motor
X-ray crystallography
title Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T17%3A52%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20Delineation%20of%20the%20Neck%20Linker%20of%20Kinesin-3%20for%20Processive%20Movement&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=Ren,%20Jinqi&rft.date=2018-07-06&rft.volume=430&rft.issue=14&rft.spage=2030&rft.epage=2041&rft.pages=2030-2041&rft.issn=0022-2836&rft.eissn=1089-8638&rft_id=info:doi/10.1016/j.jmb.2018.05.010&rft_dat=%3Cproquest_cross%3E2038273887%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2038273887&rft_id=info:pmid/29752968&rft_els_id=S0022283618304054&rfr_iscdi=true