› 1fnm

X-ray diffraction
2.8Å resolution

STRUCTURE OF THERMUS THERMOPHILUS EF-G H573A

Released:
DOI: 10.2210/pdb1fnm/pdb
PDB entry 1fnm coloured by chain, front view.
PDB entry 1fnm coloured by chain, side view.
PDB entry 1fnm coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.
Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A
J Mol Biol 303 593-603 (2000)
PMID: 11054294

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor G Chain: A
Molecule details ›
Chain: A
Length: 691 amino acids
Theoretical weight: 76.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13551 (Residues: 1-691; Coverage: 100%)
Gene names: fus, fusA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GDP 1 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 76.696Å b: 85.973Å c: 113.367Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.295
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The A-Z of bacterial translation inhibitors.
Wilson DN. (2009)
15 more

18 mentions without citation

Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu.
Agirrezabala et al. (2009)
17 more