2hxf
From Proteopedia
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[[Image:2hxf.gif|left|200px]] | [[Image:2hxf.gif|left|200px]] | ||
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'''KIF1A head-microtubule complex structure in amppnp-form''' | '''KIF1A head-microtubule complex structure in amppnp-form''' | ||
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[[Category: Hirokawa, N.]] | [[Category: Hirokawa, N.]] | ||
[[Category: Kikkawa, M.]] | [[Category: Kikkawa, M.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:49:48 2008'' | |
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Revision as of 03:49, 4 May 2008
KIF1A head-microtubule complex structure in amppnp-form
Overview
Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.
About this Structure
2HXF is a Protein complex structure of sequences from Mus musculus and Sus scrofa. Full crystallographic information is available from OCA.
Reference
High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations., Kikkawa M, Hirokawa N, EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:16946706 Page seeded by OCA on Sun May 4 06:49:48 2008