4E7Z

Myosin VI (MD) pre-powerstroke state, P21 crystal form

Summary for 4E7Z

• Entry DOI: 10.2210/pdb4e7z/pdb
• Related: 4E7S
• Descriptor: Myosin-VI, ADENOSINE-5'-DIPHOSPHATE, VANADATE ION, ... (6 entities in total)
• Functional Keywords: myosin, molecular motor, motor protein
• Biological source: Sus scrofa (pigs,swine,wild boar)
• Total number of polymer chains: 2
• Total formula weight: 183750.24

Authors

Isabet, T.,Sweeney, H.L.,Houdusse, A. (deposition date: 2012-03-19, release date: 2012-09-19, Last modification date: 2024-02-28)

Primary citation

Menetrey, J.,Isabet, T.,Ropars, V.,Mukherjea, M.,Pylypenko, O.,Liu, X.,Perez, J.,Vachette, P.,Sweeney, H.L.,Houdusse, A.M.
Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VI.
Mol.Cell, 48:75-86, 2012

PubMed Abstract: Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model.

PubMed: 22940248
DOI: 10.1016/j.molcel.2012.07.034

Experimental method

X-RAY DIFFRACTION (2.3 Å)