Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity.

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 prov

SUBMITTER: Gurel PS 

PROVIDER: S-EPMC5762158 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature