› 2z5i

X-ray diffraction
2.1Å resolution

Crystal structure of the head-to-tail junction of tropomyosin

Released:
DOI: 10.2210/pdb2z5i/pdb
PDB entry 2z5i coloured by chain, front view.
PDB entry 2z5i coloured by chain, side view.
PDB entry 2z5i coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T.
Murakami K, Stewart M, Nozawa K, Tomii K, Kudou N, Igarashi N, Shirakihara Y, Wakatsuki S, Yasunaga T, Wakabayashi T
Proc Natl Acad Sci U S A 105 7200-5 (2008)
PMID: 18483193

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-238683 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
General control transcription factor GCN4; Tropomyosin alpha-1 chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 52 amino acids
Theoretical weight: 6.06 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P58772 (Residues: 234-234, 254-284; Coverage: 11%)
  • Canonical: P03069 (Residues: 260-278; Coverage: 7%)
Gene names: AAS101, AAS3, ARG9, GCN4, TPM1, TPMA, YEL009C
Sequence domains: Basic region leucine zipper
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
General control transcription factor GCN4; Tropomyosin alpha-1 chain Chains: I, J
Molecule details ›
Chains: I, J
Length: 40 amino acids
Theoretical weight: 4.54 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P58772 (Residues: 1-24; Coverage: 9%)
  • Canonical: P03069 (Residues: 267-278; Coverage: 4%)
Gene names: AAS101, AAS3, ARG9, GCN4, TPM1, TPMA, YEL009C

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 41.957Å b: 114.498Å c: 68.351Å
α: 90° β: 107.91° γ: 90°
R-values:
R R work R free
0.219 0.217 0.246
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The streptococcal M protein: a highly versatile molecule.
Smeesters et al. (2010)
14 more

8 mentions without citation

Thin filament mutations: developing an integrative approach to a complex disorder.
Tardiff JC. (2011)
7 more