2v26 | pdb_00002v26

File:2v26.jpg

spinqualitylabelsall models 2v26, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

MYOSIN VI (MD) PRE-POWERSTROKE STATE (MG.ADP.VO4)

Overview

Due to a unique addition to the lever arm-positioning region (converter), class VI myosins move in the opposite direction (toward the minus-end of, actin filaments) compared to other characterized myosin classes. However, the large size of the myosin VI lever arm swing (powerstroke) cannot be, explained by our current view of the structural transitions that occur, within the myosin motor. We have solved the crystal structure of a, fragment of the myosin VI motor in the structural state that represents, the starting point for movement on actin; the pre-powerstroke state., Unexpectedly, the converter itself rearranges to achieve a conformation, that has not been seen for other myosins. This results in a much larger, powerstroke than is achievable without the converter rearrangement., Moreover, it provides a new mechanism that could be exploited to increase, the powerstroke of yet to be characterized plus-end-directed myosin, classes.

About this Structure

2V26 is a Single protein structure of sequence from Sus scrofa with VO4, SO4, MG, ADP and EDO as ligands. Known structural/functional Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9, BC1, BC2 and BC3. Full crystallographic information is available from OCA.

Reference

The structural basis for the large powerstroke of myosin VI., Menetrey J, Llinas P, Mukherjea M, Sweeney HL, Houdusse A, Cell. 2007 Oct 19;131(2):300-8. PMID:17956731

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