1oe9: Difference between revisions
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[[Category: unconventional myosin]] | [[Category: unconventional myosin]] | ||
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Revision as of 16:46, 30 October 2007
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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 ... [(full description)]
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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