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1sz4

From Proteopedia

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1sz4.png|left|200px]]
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==MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE==
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<StructureSection load='1sz4' size='340' side='right'caption='[[1sz4]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SZ4 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sz4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1sz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sz4 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.
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{{STRUCTURE_1sz4| PDB=1sz4 | SCENE= }}
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Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules.,Naber N, Minehardt TJ, Rice S, Chen X, Grammer J, Matuska M, Vale RD, Kollman PA, Car R, Yount RG, Cooke R, Pate E Science. 2003 May 2;300(5620):798-801. PMID:12730601<ref>PMID:12730601</ref>
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===MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12730601}}
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<div class="pdbe-citations 1sz4" style="background-color:#fffaf0;"></div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012730601</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Theoretical Model]]
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[[Category: Large Structures]]
[[Category: Car, R]]
[[Category: Car, R]]
[[Category: Chen, X]]
[[Category: Chen, X]]

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE 2'-SLADP BOUND AT THE NUCLEOTIDE SITE

PDB ID 1sz4

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