› 7pma

Electron Microscopy
3.6Å resolution

Cryo-EM structure of the actomyosin-V complex in the strong-ADP state (central 1er, class 5)

Released:
DOI: 10.2210/pdb7pma/pdb
PDB entry 7pma coloured by chain, front view.
PDB entry 7pma coloured by chain, side view.
PDB entry 7pma coloured by chain, top view.
Source organisms:
Primary publication:
High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
Pospich S, Sweeney HL, Houdusse A, Raunser S
OpenAccess logo Elife 10 (2021)
PMID: 34812732
Related structures: EMD-13526

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-146999 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Phalloidin Chain: H
Molecule details ›
Chain: H
Length: 7 amino acids
Theoretical weight: 809 Da
Source organism: Amanita phalloides
Expression system: Not provided
Myosin light chain 6B Chain: B
Molecule details ›
Chain: B
Length: 151 amino acids
Theoretical weight: 17.09 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P14649 (Residues: 58-208; Coverage: 73%)
Gene names: MLC1SA, MYL6B
Unconventional myosin-Va Chain: A
Molecule details ›
Chain: A
Length: 792 amino acids
Theoretical weight: 91.36 KDa
Source organism: Gallus gallus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02440 (Residues: 1-792; Coverage: 43%)
Gene name: MYO5A
Sequence domains:
Actin, alpha skeletal muscle Chain: C
Molecule details ›
Chain: C
Length: 377 amino acids
Theoretical weight: 42.11 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ADP 2 x ADP
3 modified residues:
Ligand DTH 1 x DTH
Ligand HYP 1 x HYP
Ligand HIC 1 x HIC

Experiments and Validation Details

Entry percentile scores
Resolution: 3.6Å
Relevant EMDB volumes: EMD-13526
Expression systems:
  • Not provided
  • Spodoptera frugiperda

Quick links

Citations

3 review citations

Actin polymerization and depolymerization in developing vertebrates.
Bai et al. (2023)
2 more

1 mention without citation

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
Pospich et al. (2021)