› 1tfe

X-ray diffraction
1.7Å resolution

DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS

Released:
DOI: 10.2210/pdb1tfe/pdb
PDB entry 1tfe coloured by chain, front view.
PDB entry 1tfe coloured by chain, side view.
PDB entry 1tfe coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus.
Jiang Y, Nock S, Nesper M, Sprinzl M, Sigler PB
Biochemistry 35 10269-78 (1996)
PMID: 8756682

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor Ts Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.73 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43895 (Residues: 55-196; Coverage: 72%)
Gene names: TTHA0860, tsf
Sequence domains: Elongation factor TS
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3121
Unit cell:
a: 60.1Å b: 60.1Å c: 94.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.207 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Production of disulfide-bonded proteins in Escherichia coli.
Berkmen M. (2012)
2 more

6 mentions without citation

Conformational changes in redox pairs of protein structures.
Fan et al. (2009)
5 more