4ZG4

Myosin Vc Pre-powerstroke

Summary for 4ZG4

• Entry DOI: 10.2210/pdb4zg4/pdb
• Descriptor: myosin-Vc, MAGNESIUM ION, VANADATE ION, ... (6 entities in total)
• Functional Keywords: myosin, pre-powerstroke, motor protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 177022.21

Authors

Ropars, V.,Pylypenko, O.,Sweeney, L.,Houdusse, A. (deposition date: 2015-04-22, release date: 2016-03-23, Last modification date: 2024-01-10)

Primary citation

Wulf, S.F.,Ropars, V.,Fujita-Becker, S.,Oster, M.,Hofhaus, G.,Trabuco, L.G.,Pylypenko, O.,Sweeney, H.L.,Houdusse, A.M.,Schroder, R.R.
Force-producing ADP state of myosin bound to actin.
Proc.Natl.Acad.Sci.USA, 113:E1844-E1852, 2016

PubMed Abstract: Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-Å cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for model building. We compare this state to the subsequent state on actin (Rigor). The ADP-bound structure reveals that the actin-binding cleft is closed, even though MgADP is tightly bound. This state is accomplished by a previously unseen conformation of the β-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5° rotation of the myosin lever arm, coupled to a β-sheet rearrangement. Thus, the structure reveals the detailed rearrangements underlying myosin force generation as well as the basis of strain-dependent ADP release that is essential for processive myosins, such as myosin V.

PubMed: 26976594
DOI: 10.1073/pnas.1516598113

Experimental method

X-RAY DIFFRACTION (2.36 Å)