4PJJ: Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4

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: 4PJJDownload
MMDB ID: 128857
PDB Deposition Date: 2014/5/12
Updated in MMDB: 2017/09
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Sus scrofa
Similar Structures:
Biological Unit for 4PJJ: dimeric; determined by author and by software (PISA)
Molecular Components in 4PJJ
Label Count Molecule
Proteins (2 molecules)
1
Unconventional Myosin-vi
Molecule annotation
1
Calmodulin(Gene symbol: Cam)
Molecule annotation
Chemicals (8 molecules)
1
1
2
1
3
2
4
2
5
2
* Click molecule labels to explore molecular sequence information.

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