1w8j

From Proteopedia

Crystal Structure Of Myosin V Motor Domain - Nucleotide-Free

PDB ID 1w8j

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Structural highlights

1w8j is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYO5A_CHICK Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Coureux PD, Sweeney HL, Houdusse A. Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:15510214