1syp: Difference between revisions
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{{Theoretical_model}} | |||
==MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITE== | |||
<StructureSection load='1syp' size='340' side='right'caption='[[1syp]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYP FirstGlance]. <br> | |||
</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=1syp FirstGlance], [https://www.ebi.ac.uk/pdbsum/1syp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syp ProSAT]</span></td></tr> | |||
</table> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1syp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Car, R]] | |||
[[Category: Chen, X]] | |||
[[Category: Cooke, R]] | |||
[[Category: Grammer, J]] | |||
[[Category: Kollman, P A]] | |||
[[Category: Matuska, M]] | |||
[[Category: Minehardt, T J]] | |||
[[Category: Naber, N]] | |||
[[Category: Pate, E]] | |||
[[Category: Rice, S]] | |||
[[Category: Vale, R D]] | |||
[[Category: Yount, R G]] | |||
Latest revision as of 10:39, 22 September 2021
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MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITEMODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND THE ELECTRON PARAMAGNETIC RESONANCE (EPR) SPIN PROBE SL-NANDP BOUND AT THE NUCLEOTIDE SITE
Structural highlights
Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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