6BNO

Structure of bare actin filament

Summary for 6BNO

• Entry DOI: 10.2210/pdb6bno/pdb
• EMDB information: 7115 7116 7117
• Descriptor: Actin, alpha skeletal muscle, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: cytoskeleton, filament, contractile protein
• Biological source: Oryctolagus cuniculus (Rabbit)
• Cellular location: Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 8
• Total formula weight: 336094.18

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

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: 29199952
DOI: 10.7554/eLife.31125

Experimental method

ELECTRON MICROSCOPY (5.5 Å)