1OE9

Crystal structure of Myosin V motor with essential light chain-nucleotide-free

Summary for 1OE9

• Entry DOI: 10.2210/pdb1oe9/pdb
• Descriptor: MYOSIN VA, MYOSIN LIGHT CHAIN 1, SLOW-TWITCH MUSCLE A ISOFORM, SULFATE ION, ... (4 entities in total)
• Functional Keywords: atpase-myosin complex, unconventional myosin, myosin v, chicken, molecular motor, atpase, elc, iq motif, muscle protein, atp-binding, atpase/myosin
• Biological source: GALLUS GALLUS (CHICKEN); More
• Total number of polymer chains: 2
• Total formula weight: 108793.51

Authors

Coureux, P.-D.,Wells, A.L.,Menetrey, J.,Yengo, C.M.,Morris, C.A.,Sweeney, H.L.,Houdusse, A. (deposition date: 2003-03-21, release date: 2003-09-26, Last modification date: 2023-12-13)

Primary citation

Coureux, P.-D.,Wells, A.L.,Menetrey, J.,Yengo, C.M.,Morris, C.A.,Sweeney, H.L.,Houdusse, A.
A Structural State of the Myosin V Motor without Bound Nucleotide
Nature, 425:419-, 2003

PubMed Abstract: 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.

PubMed: 14508494
DOI: 10.1038/NATURE01927

Experimental method

X-RAY DIFFRACTION (2.05 Å)