+Search query
-Structure paper
Title | Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity. |
---|---|
Journal, issue, pages | Elife, Vol. 6, Year 2017 |
Publish date | Dec 4, 2017 |
Authors | Pinar S Gurel / Laura Y Kim / Paul V Ruijgrok / Tosan Omabegho / Zev Bryant / Gregory M Alushin / |
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 ...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. |
External links | Elife / PubMed:29199952 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 4.6 - 7.5 Å |
Structure data | EMDB-7115, PDB-6bno: |
Chemicals | ChemComp-MG: ChemComp-ADP: |
Source |
|
Keywords | CONTRACTILE PROTEIN / Cytoskeleton / Filament / complex |