2hxh

From Proteopedia

Revision as of 09:55, 21 November 2007

KIF1A head-microtubule complex structure in adp-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

2HXH is a Protein complex structure of sequences from Mus musculus and Sus scrofa with MG, GTP, GDP, TA1 and ADP as ligands. 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

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