› 2g5i

X-ray diffraction
3.35Å resolution

Structure of tRNA-Dependent Amidotransferase GatCAB complexed with ADP-AlF4

Released:
DOI: 10.2210/pdb2g5i/pdb
PDB entry 2g5i coloured by chain, front view.
PDB entry 2g5i coloured by chain, side view.
PDB entry 2g5i coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Ammonia channel couples glutaminase with transamidase reactions in GatCAB.
Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I
Science 312 1954-8 (2006)
PMID: 16809541

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-159106 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glutamyl-tRNA(Gln) amidotransferase subunit A Chain: A
Molecule details ›
Chain: A
Length: 485 amino acids
Theoretical weight: 52.86 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P63488 (Residues: 1-485; Coverage: 100%)
Gene names: SAV1900, gatA
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B Chain: B
Molecule details ›
Chain: B
Length: 483 amino acids
Theoretical weight: 54.79 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P64201 (Residues: 1-475; Coverage: 100%)
Gene names: SAV1899, gatB
Sequence domains:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C Chain: C
Molecule details ›
Chain: C
Length: 100 amino acids
Theoretical weight: 11.28 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68807 (Residues: 1-100; Coverage: 100%)
Gene names: SAV1901, gatC
Sequence domains: Glu-tRNAGln amidotransferase C subunit
Structure domains: Glu-tRNAGln amidotransferase C subunit, N-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 76.86Å b: 85.279Å c: 183.625Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.297
Expression system: Escherichia coli

Quick links

Citations

11 review citations

From one amino acid to another: tRNA-dependent amino acid biosynthesis.
Sheppard et al. (2008)
10 more

5 mentions without citation

On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination.
Panjikar et al. (2009)
4 more