X-ray Structure of Motor and Neck Domains from Rat Brain Kinesin
We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550−554]. Novel features of the structure include the N-terminal region, folded as a β-strand, a...
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Veröffentlicht in: | Biochemistry (Easton) 1997-12, Vol.36 (51), p.16155-16165 |
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creator | Sack, Stefan Müller, Jens Marx, Alexander Thormählen, Manfred Mandelkow, Eva-Maria Brady, Scott T Mandelkow, Eckhard |
description | We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550−554]. Novel features of the structure include the N-terminal region, folded as a β-strand, and the C-terminal transition from the motor to the rod domain, folded as two β-strands plus an α-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959−966], take the form of β-strands attached to the central β-sheet of the structure. |
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The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550−554]. Novel features of the structure include the N-terminal region, folded as a β-strand, and the C-terminal transition from the motor to the rod domain, folded as two β-strands plus an α-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959−966], take the form of β-strands attached to the central β-sheet of the structure.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi9722498</identifier><identifier>PMID: 9405049</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Animals ; Brain Chemistry ; Crystallography, X-Ray ; Dimerization ; Escherichia coli - genetics ; Kinesin - chemistry ; Kinesin - genetics ; Models, Molecular ; Molecular Sequence Data ; Mutation - genetics ; Myosins - chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification</subject><ispartof>Biochemistry (Easton), 1997-12, Vol.36 (51), p.16155-16165</ispartof><rights>Copyright © 1997 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a445t-320078904415dd6aec77f47f2fe614c623e4a4b32eae9fbea8fdf33a2c060863</citedby><cites>FETCH-LOGICAL-a445t-320078904415dd6aec77f47f2fe614c623e4a4b32eae9fbea8fdf33a2c060863</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi9722498$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi9722498$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9405049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sack, Stefan</creatorcontrib><creatorcontrib>Müller, Jens</creatorcontrib><creatorcontrib>Marx, Alexander</creatorcontrib><creatorcontrib>Thormählen, Manfred</creatorcontrib><creatorcontrib>Mandelkow, Eva-Maria</creatorcontrib><creatorcontrib>Brady, Scott T</creatorcontrib><creatorcontrib>Mandelkow, Eckhard</creatorcontrib><title>X-ray Structure of Motor and Neck Domains from Rat Brain Kinesin</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550−554]. Novel features of the structure include the N-terminal region, folded as a β-strand, and the C-terminal transition from the motor to the rod domain, folded as two β-strands plus an α-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959−966], take the form of β-strands attached to the central β-sheet of the structure.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Brain Chemistry</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Escherichia coli - genetics</subject><subject>Kinesin - chemistry</subject><subject>Kinesin - genetics</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Myosins - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Rats</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM9LwzAYhoMoc04P_gFCLgoeql_SNGlu6qbzx6bihngLWZtAt7XRpAX331vZ2Enw9PHyPrwfPAgdE7ggQMnlrJCCUibTHdQlCYWISZnsoi4A8IhKDvvoIIR5GxkI1kEdySABJrvo6iPyeoUntW-yuvEGO4vHrnYe6yrHzyZb4IErdVEFbL0r8Zuu8Y1vM34qKhOK6hDtWb0M5mhze2h6dzvt30ejl-FD_3oUacaSOoopgEglMEaSPOfaZEJYJiy1hhOWcRobptkspkYbaWdGpza3caxpBhxSHvfQ2Xr207uvxoRalUXIzHKpK-OaoIRkKWEA_4KExymAJC14vgYz70LwxqpPX5TarxQB9WtVba227MlmtJmVJt-SG41tH637ItTme1trv1BcxCJR09eJGt88DunofaQGLX-65nUW1Nw1vmrV_fH3B6V8itA</recordid><startdate>19971223</startdate><enddate>19971223</enddate><creator>Sack, Stefan</creator><creator>Müller, Jens</creator><creator>Marx, Alexander</creator><creator>Thormählen, Manfred</creator><creator>Mandelkow, Eva-Maria</creator><creator>Brady, Scott T</creator><creator>Mandelkow, Eckhard</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>19971223</creationdate><title>X-ray Structure of Motor and Neck Domains from Rat Brain Kinesin</title><author>Sack, Stefan ; Müller, Jens ; Marx, Alexander ; Thormählen, Manfred ; Mandelkow, Eva-Maria ; Brady, Scott T ; Mandelkow, Eckhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-320078904415dd6aec77f47f2fe614c623e4a4b32eae9fbea8fdf33a2c060863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Brain Chemistry</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Escherichia coli - genetics</topic><topic>Kinesin - chemistry</topic><topic>Kinesin - genetics</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>Myosins - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Rats</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sack, Stefan</creatorcontrib><creatorcontrib>Müller, Jens</creatorcontrib><creatorcontrib>Marx, Alexander</creatorcontrib><creatorcontrib>Thormählen, Manfred</creatorcontrib><creatorcontrib>Mandelkow, Eva-Maria</creatorcontrib><creatorcontrib>Brady, Scott T</creatorcontrib><creatorcontrib>Mandelkow, Eckhard</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sack, Stefan</au><au>Müller, Jens</au><au>Marx, Alexander</au><au>Thormählen, Manfred</au><au>Mandelkow, Eva-Maria</au><au>Brady, Scott T</au><au>Mandelkow, Eckhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>X-ray Structure of Motor and Neck Domains from Rat Brain Kinesin</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1997-12-23</date><risdate>1997</risdate><volume>36</volume><issue>51</issue><spage>16155</spage><epage>16165</epage><pages>16155-16165</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550−554]. Novel features of the structure include the N-terminal region, folded as a β-strand, and the C-terminal transition from the motor to the rod domain, folded as two β-strands plus an α-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959−966], take the form of β-strands attached to the central β-sheet of the structure.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>9405049</pmid><doi>10.1021/bi9722498</doi><tpages>11</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Brain Chemistry Crystallography, X-Ray Dimerization Escherichia coli - genetics Kinesin - chemistry Kinesin - genetics Models, Molecular Molecular Sequence Data Mutation - genetics Myosins - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Rats Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification |
title | X-ray Structure of Motor and Neck Domains from Rat Brain Kinesin |
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