1oe9

File:1oe9.gif

spinqualitylabelsall models 1oe9, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITH ESSENTIAL LIGHT CHAIN- NUCLEOTIDE-FREE

OverviewOverview

The myosin superfamily of molecular motors use ATP hydrolysis and, actin-activated product release to produce directed movement and force., Although this is generally thought to involve movement of a mechanical, lever arm attached to a motor core, the structural details of the, rearrangement in myosin that drive the lever arm motion on actin, attachment are unknown. Motivated by kinetic evidence that the processive, unconventional myosin, myosin V, populates a unique state in the absence, of nucleotide and actin, we obtained a 2.0 A structure of a myosin V, fragment. Here we reveal a conformation of myosin without bound, nucleotide. The nucleotide-binding site has adopted new conformations of, the nucleotide-binding elements that reduce the affinity for the, nucleotide. The major cleft in the molecule has closed, and the lever arm, has assumed a position consistent with that in an actomyosin rigor, complex. These changes have been accomplished by relative movements of the, subdomains of the molecule, and reveal elements of the structural, communication between the actin-binding interface and nucleotide-binding, site of myosin that underlie the mechanism of chemo-mechanical, transduction.

About this StructureAbout this Structure

1OE9 is a Protein complex structure of sequences from Gallus gallus and Homo sapiens with SO4 as ligand. Structure known Active Site: ATP. Full crystallographic information is available from OCA.

ReferenceReference

A structural state of the myosin V motor without bound nucleotide., Coureux PD, Wells AL, Menetrey J, Yengo CM, Morris CA, Sweeney HL, Houdusse A, Nature. 2003 Sep 25;425(6956):419-23. PMID:14508494

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