› 2otg

X-ray diffraction
3.12Å resolution

Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor

Released:
DOI: 10.2210/pdb2otg/pdb
PDB entry 2otg coloured by chain, front view.
PDB entry 2otg coloured by chain, side view.
PDB entry 2otg coloured by chain, top view.
Source organism: Placopecten magellanicus
Primary publication:
Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor.
Yang Y, Gourinath S, Kovács M, Nyitray L, Reutzel R, Himmel DM, O'Neall-Hennessey E, Reshetnikova L, Szent-Györgyi AG, Brown JH, Cohen C
Structure 15 553-64 (2007)
PMID: 17502101

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173237 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Myosin heavy chain Chain: A
Molecule details ›
Chain: A
Length: 840 amino acids
Theoretical weight: 96.14 KDa
Source organism: Placopecten magellanicus
UniProt:
  • Canonical: Q26080 (Residues: 1-840; Coverage: 43%)
Sequence domains:
EF-hand domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 157 amino acids
Theoretical weight: 17.77 KDa
Source organism: Placopecten magellanicus
UniProt:
  • Canonical: Q26068 (Residues: 1-157; Coverage: 100%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
EF-hand domain-containing protein Chain: C
Molecule details ›
Chain: C
Length: 157 amino acids
Theoretical weight: 17.81 KDa
Source organism: Placopecten magellanicus
UniProt:
  • Canonical: Q26066 (Residues: 1-157; Coverage: 100%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand ADP 1 x ADP
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 87.087Å b: 51.689Å c: 159.9Å
α: 90° β: 100.77° γ: 90°
R-values:
R R work R free
0.276 0.276 0.304

Quick links

Citations

9 review citations

Structural and functional insights into the Myosin motor mechanism.
Sweeney et al. (2010)
8 more

5 mentions without citation

The hypertrophic cardiomyopathy myosin mutation R453C alters ATP binding and hydrolysis of human cardiac β-myosin.
Bloemink et al. (2014)
4 more