1goj

From Proteopedia

Revision as of 13:18, 18 December 2007

STRUCTURE OF A FAST KINESIN: IMPLICATIONS FOR ATPASE MECHANISM AND INTERACTIONS WITH MICROTUBULES

Overview

We determined the crystal structure of the motor domain of the fast fungal, kinesin from Neurospora crassa (NcKin). The structure has several unique, features. (i) Loop 11 in the switch 2 region is ordered and enables one to, describe the complete nucleotide-binding pocket, including three, inter-switch salt bridges between switch 1 and 2. (ii) Loop 9 in the, switch 1 region bends outwards, making the nucleotide-binding pocket very, wide. The displacement in switch 1 resembles that of the G-protein ras, complexed with its guanosine nucleotide exchange factor. (iii) Loop 5 in, the entrance to the nucleotide-binding pocket is remarkably long and, interacts with the ribose of ATP. (iv) The linker and neck region is not, well defined, indicating that it is mobile. (v) Image reconstructions of, ice-embedded microtubules decorated with NcKin show that it interacts with, several tubulin subunits, including a central beta-tubulin monomer and the, two flanking alpha-tubulin monomers within the microtubule protofilament., Comparison of NcKin with other kinesins, myosin and G-proteins suggests, that the rate-limiting step of ADP release is accelerated in the fungal, kinesin and accounts for the unusually high velocity and ATPase activity.

About this Structure

1GOJ is a Single protein structure of sequence from Neurospora crassa with MG and ADP as ligands. Active as Plus-end-directed kinesin ATPase, with EC number 3.6.4.4 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules., Song YH, Marx A, Muller J, Woehlke G, Schliwa M, Krebs A, Hoenger A, Mandelkow E, EMBO J. 2001 Nov 15;20(22):6213-25. PMID:11707393

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