2bkh: Difference between revisions

Revision as of 18:06, 27 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:2bkh.png

Template:STRUCTURE 2bkh

MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTUREMYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE

Template:ABSTRACT PUBMED 15944696

About this StructureAbout this Structure

2BKH is a Protein complex structure of sequences from Drosophila melanogaster and Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

The structure of the myosin VI motor reveals the mechanism of directionality reversal., Menetrey J, Bahloul A, Wells AL, Yengo CM, Morris CA, Sweeney HL, Houdusse A, Nature. 2005 Jun 9;435(7043):779-85. PMID:15944696

Page seeded by OCA on Sun Jul 27 18:06:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2bkh.gif|left|200px]]
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-'''MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE'''
+===MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE===
-==Overview==
+<!--
-Here we solve a 2.4-A structure of a truncated version of the reverse-direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulin molecules. The structure reveals only minor differences in the motor domain from that in plus-end directed myosins, with the exception of two unique inserts. The first is near the nucleotide-binding pocket and alters the rates of nucleotide association and dissociation. The second unique insert forms an integral part of the myosin VI converter domain along with a calmodulin bound to a novel target motif within the insert. This serves to redirect the effective 'lever arm' of myosin VI, which includes a second calmodulin bound to an 'IQ motif', towards the pointed (minus) end of the actin filament. This repositioning largely accounts for the reverse directionality of this class of myosin motors. We propose a model incorporating a kinesin-like uncoupling/docking mechanism to provide a full explanation of the movements of myosin VI.
+The line below this paragraph, {{ABSTRACT_PUBMED_15944696}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15944696 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15944696}}
 ==About this Structure==
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 [[Category: Nucleotide-free conformation]]
 [[Category: Reverse myosin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:24:47 2008''
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