› 1ytz

X-ray diffraction
3Å resolution

Crystal structure of skeletal muscle troponin in the Ca2+-activated state

Released:
DOI: 10.2210/pdb1ytz/pdb
PDB entry 1ytz coloured by chain, front view.
PDB entry 1ytz coloured by chain, side view.
PDB entry 1ytz coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Ca(2+)-regulated structural changes in troponin.
Vinogradova MV, Stone DB, Malanina GG, Karatzaferi C, Cooke R, Mendelson RA, Fletterick RJ
Proc Natl Acad Sci U S A 102 5038-43 (2005)
PMID: 15784741

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-135943 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Troponin T, fast skeletal muscle isoforms Chain: T
Molecule details ›
Chain: T
Length: 107 amino acids
Theoretical weight: 12.69 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12620 (Residues: 157-263; Coverage: 41%)
Gene name: TNNT3
Sequence domains: Troponin
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Troponin I, fast skeletal muscle Chain: I
Molecule details ›
Chain: I
Length: 182 amino acids
Theoretical weight: 21.12 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68246 (Residues: 2-183; Coverage: 100%)
Gene name: TNNI2
Sequence domains: Troponin
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Troponin C, skeletal muscle Chain: C
Molecule details ›
Chain: C
Length: 162 amino acids
Theoretical weight: 18.26 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02588 (Residues: 2-163; Coverage: 99%)
Gene name: TNNC2
Sequence domains:
Structure domains: EF-hand

Ligands and Environments

2 bound ligands:
Ligand DR6 3 x DR6
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P43212
Unit cell:
a: 138.608Å b: 138.608Å c: 83.676Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.289 0.338
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

32 review citations

Structural basis for diversity of the EF-hand calcium-binding proteins.
Grabarek Z. (2006)
31 more

37 mentions without citation

TNNI1, TNNI2 and TNNI3: Evolution, regulation, and protein structure-function relationships.
Sheng et al. (2016)
36 more