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2V26

Myosin VI (MD) pre-powerstroke state (Mg.ADP.VO4)

Summary for 2V26
Entry DOI10.2210/pdb2v26/pdb
Related2BKH 2BKI
DescriptorMYOSIN VI, ADENOSINE-5'-DIPHOSPHATE, VANADATE ION, ... (7 entities in total)
Functional Keywordscalmodulin-binding, nucleotide-binding, myosin, membrane, vanadate, myosin vi, transport, pre- powerstroke, transition state, protein transport, actin-binding, motor protein, nuclear protein, endocytosis, atp-binding, coiled coil, domain motor, golgi apparatus, phosphorylation, molecular motor, structural protein
Biological sourceSUS SCROFA (PIG)
Cellular locationGolgi apparatus, trans-Golgi network membrane; Peripheral membrane protein (By similarity): Q29122
Total number of polymer chains1
Total formula weight90625.80
Authors
Menetrey, J.,Llinas, P.,Mukherjea, M.,Sweeney, H.L.,Houdusse, A. (deposition date: 2007-06-03, release date: 2007-11-20, Last modification date: 2023-12-13)
Primary citationMenetrey, J.,Llinas, P.,Mukherjea, M.,Sweeney, H.L.,Houdusse, A.
The Structural Basis for the Large Powerstroke of Myosin Vi.
Cell(Cambridge,Mass.), 131:300-, 2007
Cited by
PubMed Abstract: Due to a unique addition to the lever arm-positioning region (converter), class VI myosins move in the opposite direction (toward the minus-end of actin filaments) compared to other characterized myosin classes. However, the large size of the myosin VI lever arm swing (powerstroke) cannot be explained by our current view of the structural transitions that occur within the myosin motor. We have solved the crystal structure of a fragment of the myosin VI motor in the structural state that represents the starting point for movement on actin; the pre-powerstroke state. Unexpectedly, the converter itself rearranges to achieve a conformation that has not been seen for other myosins. This results in a much larger powerstroke than is achievable without the converter rearrangement. Moreover, it provides a new mechanism that could be exploited to increase the powerstroke of yet to be characterized plus-end-directed myosin classes.
PubMed: 17956731
DOI: 10.1016/J.CELL.2007.08.027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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