1w8j
From Proteopedia
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| - | [[Image:1w8j.gif|left|200px]] | + | [[Image:1w8j.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF MYOSIN V MOTOR DOMAIN-NUCLEOTIDE-FREE''' | + | {{Structure |
| + | |PDB= 1w8j |SIZE=350|CAPTION= <scene name='initialview01'>1w8j</scene>, resolution 2.7Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+D'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF MYOSIN V MOTOR DOMAIN-NUCLEOTIDE-FREE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W8J is a [ | + | 1W8J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8J OCA]. |
==Reference== | ==Reference== | ||
| - | Three myosin V structures delineate essential features of chemo-mechanical transduction., Coureux PD, Sweeney HL, Houdusse A, EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:[http:// | + | Three myosin V structures delineate essential features of chemo-mechanical transduction., Coureux PD, Sweeney HL, Houdusse A, EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15510214 15510214] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: unconventional myosin]] | [[Category: unconventional myosin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:41 2008'' |
Revision as of 12:53, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MYOSIN V MOTOR DOMAIN-NUCLEOTIDE-FREE
Overview
The molecular motor, myosin, undergoes conformational changes in order to convert chemical energy into force production. Based on kinetic and structural considerations, we assert that three crystal forms of the myosin V motor delineate the conformational changes that myosin motors undergo upon detachment from actin. First, a motor domain structure demonstrates that nucleotide-free myosin V adopts a specific state (rigor-like) that is not influenced by crystal packing. A second structure reveals an actomyosin state that favors rapid release of ADP, and differs from the rigor-like state by a P-loop rearrangement. Comparison of these structures with a third structure, a 2.0 angstroms resolution structure of the motor bound to an ATP analog, illuminates the structural features that provide communication between the actin interface and nucleotide-binding site. Paramount among these is a region we name the transducer, which is composed of the seven-stranded beta-sheet and associated loops and linkers. Reminiscent of the beta-sheet distortion of the F1-ATPase, sequential distortion of this transducer region likely controls sequential release of products from the nucleotide pocket during force generation.
About this Structure
1W8J is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Three myosin V structures delineate essential features of chemo-mechanical transduction., Coureux PD, Sweeney HL, Houdusse A, EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:15510214
Page seeded by OCA on Thu Mar 20 14:53:41 2008
