› 2zyj

X-ray diffraction
1.67Å resolution

Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-glutamate), from Thermus thermophilus HB27

Released:
DOI: 10.2210/pdb2zyj/pdb
PDB entry 2zyj coloured by chain, front view.
PDB entry 2zyj coloured by chain, side view.
PDB entry 2zyj coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-aminoadipate aminotransferase from Thermus thermophilus.
Ouchi T, Tomita T, Miyagawa T, Kuzuyama T, Nishiyama M
Biochem Biophys Res Commun 388 21-7 (2009)
PMID: 19632206

Function and Biology Details

Reaction catalysed: 
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-aminoadipate transaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 43.9 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72LL6 (Residues: 1-397; Coverage: 100%)
Gene names: TT_C0043, lysN
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 55.761Å b: 93.346Å c: 150.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.246
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure, function, and regulation of enzymes involved in amino acid metabolism of bacteria and archaea.
Tomita T. (2017)
3 other articles

1 mention without citation

Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.
Peña-Soler et al. (2014)