4PFP: Myosin Vi Motor Domain In The Pi Release State (with Pi) Space Group P21

Citation:
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.
PDB ID: 4PFPDownload
MMDB ID: 128855
PDB Deposition Date: 2014/4/30
Updated in MMDB: 2017/09
Experimental Method:
x-ray diffraction
Resolution: 2.32  Å
Source Organism:
Similar Structures:
Biological Unit for 4PFP: dimeric; determined by software (PISA)
Molecular Components in 4PFP
Label Count Molecule
Proteins (2 molecules)
2
Unconventional Myosin-vi
Molecule annotation
Chemicals (8 molecules)
1
2
2
2
3
1
4
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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