2V26
Myosin VI (MD) pre-powerstroke state (Mg.ADP.VO4)
Summary for 2V26
Entry DOI | 10.2210/pdb2v26/pdb |
Related | 2BKH 2BKI |
Descriptor | MYOSIN VI, ADENOSINE-5'-DIPHOSPHATE, VANADATE ION, ... (7 entities in total) |
Functional Keywords | calmodulin-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 source | SUS SCROFA (PIG) |
Cellular location | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein (By similarity): Q29122 |
Total number of polymer chains | 1 |
Total formula weight | 90625.80 |
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 citation | Menetrey, 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: 17956731DOI: 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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