4PJL

Myosin VI motor domain A458E mutant in the Pi release state, space group P212121 -

Summary for 4PJL

• Entry DOI: 10.2210/pdb4pjl/pdb
• Related: 4PFO
• Descriptor: Unconventional myosin-VI, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: motor protein, myosin vi, motor domain, pi release state
• Biological source: Sus scrofa (Pig)
• Total number of polymer chains: 1
• Total formula weight: 91461.84

Authors

Isabet, T.,Benisty, H.,Llinas, P.,Sweeney, H.L.,Houdusse, A. (deposition date: 2014-05-12, release date: 2015-04-29, Last modification date: 2023-12-20)

Primary citation

Llinas, P.,Isabet, T.,Song, L.,Ropars, V.,Zong, B.,Benisty, H.,Sirigu, S.,Morris, C.,Kikuti, C.,Safer, D.,Sweeney, H.L.,Houdusse, A.
How actin initiates the motor activity of Myosin.
Dev.Cell, 33:401-412, 2015

PubMed Abstract: Fundamental to cellular processes are directional movements driven by molecular motors. A common theme for these and other molecular machines driven by ATP is that controlled release of hydrolysis products is essential for using the chemical energy efficiently. Mechanochemical transduction by myosin motors on actin is coupled to unknown structural changes that result in the sequential release of inorganic phosphate (Pi) and MgADP. We present here a myosin structure possessing an actin-binding interface and a tunnel (back door) that creates an escape route for Pi with a minimal rotation of the myosin lever arm that drives movements. We propose that this state represents the beginning of the powerstroke on actin and that Pi translocation from the nucleotide pocket triggered by actin binding initiates myosin force generation. This elucidates how actin initiates force generation and movement and may represent a strategy common to many molecular machines.

PubMed: 25936506
DOI: 10.1016/j.devcel.2015.03.025

Experimental method

X-RAY DIFFRACTION (2.1 Å)