2o0a
From Proteopedia
The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.
Overview
Conventional kinesin and class V and VI myosins coordinate the mechanochemical cycles of their motor domains for processive movement of cargo along microtubules or actin filaments. It is widely accepted that this coordination is achieved by allosteric communication or mechanical strain between the motor domains, which controls the nucleotide state and interaction with microtubules or actin. However, questions remain about the interplay between the strain and the nucleotide state. We present an analysis of Saccharomyces cerevisiae Kar3/Vik1, a heterodimeric C-terminal Kinesin-14 containing catalytic Kar3 and the nonmotor protein Vik1. The X-ray crystal structure of Vik1 exhibits a similar fold to the kinesin and myosin catalytic head, but lacks an ATP binding site. Vik1 binds more tightly to microtubules than Kar3 and facilitates cooperative microtubule decoration by Kar3/Vik1 heterodimers, and yet allows motility. These results demand communication between Vik1 and Kar3 via a mechanism that coordinates their interactions with microtubules.
About this Structure
2O0A is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site., Allingham JS, Sproul LR, Rayment I, Gilbert SP, Cell. 2007 Mar 23;128(6):1161-72. PMID:17382884 Page seeded by OCA on Sun May 4 10:08:50 2008
