1mkj

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[[Image:1mkj.gif|left|200px]]
[[Image:1mkj.gif|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkj OCA], [http://www.ebi.ac.uk/pdbsum/1mkj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mkj RCSB]</span>
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'''Human Kinesin Motor Domain With Docked Neck Linker'''
'''Human Kinesin Motor Domain With Docked Neck Linker'''
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[[Category: Rice, S.]]
[[Category: Rice, S.]]
[[Category: Sindelar, C V.]]
[[Category: Sindelar, C V.]]
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[[Category: atpase]]
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[[Category: Atpase]]
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[[Category: microtubule]]
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[[Category: Microtubule]]
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[[Category: motor protein]]
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[[Category: Motor protein]]
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[[Category: myosin]]
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[[Category: Myosin]]
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[[Category: neck linker]]
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[[Category: Neck linker]]
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[[Category: relay helix]]
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[[Category: Relay helix]]
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[[Category: switch ii]]
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[[Category: Switch ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:18:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:20 2008''
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Revision as of 22:18, 2 May 2008

Template:STRUCTURE 1mkj

Human Kinesin Motor Domain With Docked Neck Linker


Overview

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

1MKJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 01:18:09 2008

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