1mkj: Difference between revisions
New page: left|200px<br /> <applet load="1mkj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mkj, resolution 2.70Å" /> '''Human Kinesin Motor... |
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[[Image:1mkj.gif|left|200px]]<br /> | [[Image:1mkj.gif|left|200px]]<br /><applet load="1mkj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1mkj, resolution 2.70Å" /> | caption="1mkj, resolution 2.70Å" /> | ||
'''Human Kinesin Motor Domain With Docked Neck Linker'''<br /> | '''Human Kinesin Motor Domain With Docked Neck Linker'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of the molecular motor kinesin show conformational | Crystal structures of the molecular motor kinesin show conformational variability in a structural element called the neck linker. Conformational change in the neck linker, initiated by ATP exchange, is thought to drive the movement of kinesin along the microtubule track. We use site-specific EPR measurements to show that when microtubules are absent, the neck linker exists in equilibrium between two structural states (disordered and 'docked'). The active site nucleotide does not control the position taken by the neck linker. However, we find that sulfate can specifically bind near the nucleotide site and stabilize the docked neck linker conformation, which we confirmed by solving a new crystal structure. Comparing the crystal structures of our construct with the docked or undocked neck linker reveals how microtubule binding may activate the nucleotide-sensing mechanism of kinesin, allowing neck linker transitions to power motility. | ||
==About this Structure== | ==About this Structure== | ||
1MKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, SO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1MKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</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=1MKJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Budny, M | [[Category: Budny, M J.]] | ||
[[Category: Cooke, R.]] | [[Category: Cooke, R.]] | ||
[[Category: Fletterick, R.]] | [[Category: Fletterick, R.]] | ||
[[Category: Naber, N.]] | [[Category: Naber, N.]] | ||
[[Category: Rice, S.]] | [[Category: Rice, S.]] | ||
[[Category: Sindelar, C | [[Category: Sindelar, C V.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: switch ii]] | [[Category: switch ii]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:07 2008'' | ||
Revision as of 14:56, 21 February 2008
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Human Kinesin Motor Domain With Docked Neck Linker
OverviewOverview
Crystal structures of the molecular motor kinesin show conformational variability in a structural element called the neck linker. Conformational change in the neck linker, initiated by ATP exchange, is thought to drive the movement of kinesin along the microtubule track. We use site-specific EPR measurements to show that when microtubules are absent, the neck linker exists in equilibrium between two structural states (disordered and 'docked'). The active site nucleotide does not control the position taken by the neck linker. However, we find that sulfate can specifically bind near the nucleotide site and stabilize the docked neck linker conformation, which we confirmed by solving a new crystal structure. Comparing the crystal structures of our construct with the docked or undocked neck linker reveals how microtubule binding may activate the nucleotide-sensing mechanism of kinesin, allowing neck linker transitions to power motility.
About this StructureAbout this Structure
1MKJ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy., Sindelar CV, Budny MJ, Rice S, Naber N, Fletterick R, Cooke R, Nat Struct Biol. 2002 Nov;9(11):844-8. PMID:12368902
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