1vfx

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(New page: 200px<br /><applet load="1vfx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfx, resolution 2.55&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx'''<br />
'''Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx'''<br />
==Overview==
==Overview==
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The motor protein kinesin moves along microtubules, driven by adenosine, triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin, converts the chemical energy into mechanical movement. We report crystal, structures of monomeric kinesin KIF1A with three transition-state analogs:, adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with, known structures of the ADP-bound state and the, adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show, that kinesin uses two microtubule-binding loops in an alternating manner, to change its interaction with microtubules during the ATP hydrolysis, cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is, extended in the ADP structure. ADP-vanadate displays an intermediate, structure in which a conformational change in two switch regions causes, both loops to be raised from the microtubule, thus actively detaching, kinesin.
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The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.
==About this Structure==
==About this Structure==
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1VFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, AF3, TRS and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFX OCA].
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1VFX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=AF3:'>AF3</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFX OCA].
==Reference==
==Reference==
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[[Category: motor]]
[[Category: motor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:48:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:51 2008''

Revision as of 13:34, 21 February 2008

Image:1vfx.gif

1vfx, resolution 2.55Å

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Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx

Overview

The motor protein kinesin moves along microtubules, driven by adenosine triphosphate (ATP) hydrolysis. However, it remains unclear how kinesin converts the chemical energy into mechanical movement. We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). These structures, together with known structures of the ADP-bound state and the adenylyl-(beta,gamma-methylene) diphosphate (AMP-PCP)-bound state, show that kinesin uses two microtubule-binding loops in an alternating manner to change its interaction with microtubules during the ATP hydrolysis cycle; loop L11 is extended in the AMP-PNP structure, whereas loop L12 is extended in the ADP structure. ADP-vanadate displays an intermediate structure in which a conformational change in two switch regions causes both loops to be raised from the microtubule, thus actively detaching kinesin.

About this Structure

1VFX is a Single protein structure of sequence from Mus musculus with , , and as ligands. Full crystallographic information is available from OCA.

Reference

KIF1A alternately uses two loops to bind microtubules., Nitta R, Kikkawa M, Okada Y, Hirokawa N, Science. 2004 Jul 30;305(5684):678-83. PMID:15286375

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