› 1uc9

X-ray diffraction
2.38Å resolution

Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1uc9/pdb
PDB entry 1uc9 coloured by chain, front view.
PDB entry 1uc9 coloured by chain, side view.
PDB entry 1uc9 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8.
Sakai H, Vassylyeva MN, Matsuura T, Sekine Si, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S
J Mol Biol 332 729-40 (2003)
PMID: 12963379

Function and Biology Details

Reaction catalysed: 
ATP + [amino-group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177837 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-aminoadipate--LysW ligase LysX Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 30.43 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SH23 (Residues: 1-280; Coverage: 100%)
Gene names: TTHA1907, lysX
Sequence domains: RimK-like ATP-grasp domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: C2
Unit cell:
a: 126.591Å b: 52.145Å c: 105.105Å
α: 90° β: 123.24° γ: 90°
R-values:
R R work R free
0.243 0.243 0.28
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The ATP-grasp enzymes.
Fawaz et al. (2011)
2 more

2 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
1 more