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TitleCryo-EM structure of the autoinhibited state of myosin-2.
Journal, issue, pagesSci Adv, Vol. 7, Issue 52, Page eabk3273, Year 2021
Publish dateDec 24, 2021
AuthorsSarah M Heissler / Amandeep S Arora / Neil Billington / James R Sellers / Krishna Chinthalapudi /
PubMed AbstractWe solved the near-atomic resolution structure of smooth muscle myosin-2 in the autoinhibited state (10) using single-particle cryo–electron microscopy. The 3.4-Å structure reveals the precise ...We solved the near-atomic resolution structure of smooth muscle myosin-2 in the autoinhibited state (10) using single-particle cryo–electron microscopy. The 3.4-Å structure reveals the precise molecular architecture of 10 and the structural basis for myosin-2 regulation. We reveal the position of the phosphorylation sites that control myosin autoinhibition and activation by phosphorylation of the regulatory light chain. Further, we present a previously unidentified conformational state in myosin-2 that traps ADP and P produced by the hydrolysis of ATP in the active site. This noncanonical state represents a branch of the myosin enzyme cycle and explains the autoinhibition of the enzyme function of 10 along with its reduced affinity for actin. Together, our structure defines the molecular mechanisms that drive 10 formation, stabilization, and relief by phosphorylation of the regulatory light chain.
External linksSci Adv / PubMed:34936462 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

EMDB-23810, PDB-7mf3:
Structure of the autoinhibited state of smooth muscle myosin-2
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MG:
Unknown entry

Source
  • gallus gallus (chicken)
KeywordsCONTRACTILE PROTEIN / Muscle contraction / ATPase / autoinhibition / 10S

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