6BNP
CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state
Summary for 6BNP
| Entry DOI | 10.2210/pdb6bnp/pdb |
| EMDB information | 7115 7116 7117 |
| Descriptor | Unconventional myosin-VI, Actin, alpha skeletal muscle, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | cytoskeleton, filament, complex, contractile protein |
| Biological source | Sus scrofa (Pig) More |
| Cellular location | Cytoplasm, cytoskeleton: P68135 |
| Total number of polymer chains | 14 |
| Total formula weight | 815118.38 |
| Authors | Gurel, P.S.,Alushin, G.A. (deposition date: 2017-11-17, release date: 2018-01-10, Last modification date: 2024-03-13) |
| Primary citation | Gurel, P.S.,Kim, L.Y.,Ruijgrok, P.V.,Omabegho, T.,Bryant, Z.,Alushin, G.M. Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity. Elife, 6:-, 2017 Cited by PubMed Abstract: Despite extensive scrutiny of the myosin superfamily, the lack of high-resolution structures of actin-bound states has prevented a complete description of its mechanochemical cycle and limited insight into how sequence and structural diversification of the motor domain gives rise to specialized functional properties. Here we present cryo-EM structures of the unique minus-end directed myosin VI motor domain in rigor (4.6 Å) and Mg-ADP (5.5 Å) states bound to F-actin. Comparison to the myosin IIC-F-actin rigor complex reveals an almost complete lack of conservation of residues at the actin-myosin interface despite preservation of the primary sequence regions composing it, suggesting an evolutionary path for motor specialization. Additionally, analysis of the transition from ADP to rigor provides a structural rationale for force sensitivity in this step of the mechanochemical cycle. Finally, we observe reciprocal rearrangements in actin and myosin accompanying the transition between these states, supporting a role for actin structural plasticity during force generation by myosin VI. PubMed: 29199952DOI: 10.7554/eLife.31125 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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