1syj: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}
{{Seed}}
[[Image:1syj.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 SSL-NANDP BOUND AT THE NUCLEOTIDE SITE==
The line below this paragraph, containing "STRUCTURE_1syj", creates the "Structure Box" on the page.
<StructureSection load='1syj' size='340' side='right'caption='[[1syj]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYJ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=1syj FirstGlance], [https://www.ebi.ac.uk/pdbsum/1syj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syj ProSAT]</span></td></tr>
-->
</table>
{{STRUCTURE_1syj|  PDB=1syj  |  SCENE=  }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SSL-NANDP BOUND AT THE NUCLEOTIDE SITE===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_12730601}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1syj" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 12730601 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12730601}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYJ OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:12730601</ref><references group="xtra"/>
[[Category: Car, R]]
[[Category: Car, R]]
[[Category: Chen, X]]
[[Category: Chen, X]]
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[[Category: Vale, R D]]
[[Category: Vale, R D]]
[[Category: Yount, R G]]
[[Category: Yount, R G]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:33:43 2010''

Latest revision as of 07:39, 22 September 2021

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 SSL-NANDP BOUND AT THE NUCLEOTIDE SITE

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