1oe9: Difference between revisions

Revision as of 04:09, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oe9.png

Template:STRUCTURE 1oe9

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

Template:ABSTRACT PUBMED 14508494

About this StructureAbout this Structure

1OE9 is a Protein complex structure of sequences from Gallus gallus and Homo sapiens. 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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-[[Image:1oe9.gif|left|200px]]
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 {{STRUCTURE_1oe9|  PDB=1oe9  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITH ESSENTIAL LIGHT CHAIN- NUCLEOTIDE-FREE'''
+===CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITH ESSENTIAL LIGHT CHAIN- NUCLEOTIDE-FREE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14508494}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14508494 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14508494}}
 ==About this Structure==
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 [[Category: Myosin v]]
 [[Category: Unconventional myosin]]
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