2VAS

Myosin VI (MD-insert2-CaM, Delta-Insert1) Post-rigor state

Summary for 2VAS

• Entry DOI: 10.2210/pdb2vas/pdb
• Related: 2BKH 2BKI 2V26
• Descriptor: MYOSIN VI, CALMODULIN, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: calmodulin-binding, nucleotide-binding, transport, calmodulin, endocytosis, mg.adp.befx, cam, myosin, nucleus, membrane, myosin vi, cytoplasm, golgi apparatus, phosphorylation, molecular motor, atp-binding, coiled coil, actin-binding, motor protein, post-rigor state, protein transport
• Biological source: SUS SCROFA (PIG); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein (By similarity): Q29122
• Total number of polymer chains: 2
• Total formula weight: 107402.82

Authors

Menetrey, J.,Llinas, P.,Cicolari, J.,Squires, G.,Liu, X.,Li, A.,Sweeney, H.L.,Houdusse, A. (deposition date: 2007-09-04, release date: 2007-12-11, Last modification date: 2023-12-13)

Primary citation

Menetrey, J.,Llinas, P.,Cicolari, J.,Squires, G.,Liu, X.,Li, A.,Sweeney, H.L.,Houdusse, A.
The Post-Rigor Structure of Myosin Vi and Implications for the Recovery Stroke.
Embo J., 27:244-, 2008

PubMed Abstract: Myosin VI has an unexpectedly large swing of its lever arm (powerstroke) that optimizes its unique reverse direction movement. The basis for this is an unprecedented rearrangement of the subdomain to which the lever arm is attached, referred to as the converter. It is unclear at what point(s) in the myosin VI ATPase cycle rearrangements in the converter occur, and how this would effect lever arm position. We solved the structure of myosin VI with an ATP analogue (ADP.BeF3) bound in its nucleotide-binding pocket. The structure reveals that no rearrangement in the converter occur upon ATP binding. Based on previously solved myosin structures, our structure suggests that no reversal of the powerstroke occurs during detachment of myosin VI from actin. The structure also reveals novel features of the myosin VI motor that may be important in maintaining the converter conformation during detachment from actin, and other features that may promote rapid rearrangements in the structure following actin detachment that enable hydrolysis of ATP.

PubMed: 18046460
DOI: 10.1038/SJ.EMBOJ.7601937

Experimental method

X-RAY DIFFRACTION (2.4 Å)