1w7j
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The molecular motor, myosin, undergoes conformational changes in order to | + | 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== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Coureux, P | + | [[Category: Coureux, P D.]] |
[[Category: Houdusse, A.]] | [[Category: Houdusse, A.]] | ||
| - | [[Category: Sweeney, H | + | [[Category: Sweeney, H L.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: BEF]] | [[Category: BEF]] | ||
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[[Category: unconventional myosin]] | [[Category: unconventional myosin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:16 2008'' |
Revision as of 13:41, 21 February 2008
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CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITH ESSENTIAL LIGHT CHAIN + ADP-BEFX- NEAR RIGOR
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
1W7J is a Protein complex structure of sequences from Gallus gallus and Homo sapiens with , and as ligands. Known structural/functional Site: . 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 Feb 21 15:41:16 2008
Categories: Gallus gallus | Homo sapiens | Protein complex | Coureux, P D. | Houdusse, A. | Sweeney, H L. | ADP | BEF | MG | Actin-binding | Atp-binding | Atpase | Calmodulin-binding | Chicken | Direct protein sequencing | Elc | Iq motif | Molecular motor | Muscle protein | Myosin | Myosin v | Phosphorylation | Unconventional myosin
