› 3a3u

X-ray diffraction
1.65Å resolution

Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb3a3u/pdb
PDB entry 3a3u coloured by chain, front view.
PDB entry 3a3u coloured by chain, side view.
PDB entry 3a3u coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8.
Arai R, Murayama K, Uchikubo-Kamo T, Nishimoto M, Toyama M, Kuramitsu S, Terada T, Shirouzu M, Yokoyama S
J Struct Biol 168 575-81 (2009)
PMID: 19602440

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,4-dihydroxy-6-naphtoate synthase Chain: A
Molecule details ›
Chain: A
Length: 272 amino acids
Theoretical weight: 30.07 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SI12 (Residues: 1-272; Coverage: 100%)
Gene names: TTHA1568, mqnD
Sequence domains: Menaquinone biosynthesis
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

3 bound ligands:
Ligand K 1 x K
Ligand TLA 1 x TLA
Ligand 7PE 1 x 7PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P43212
Unit cell:
a: 60.196Å b: 60.196Å c: 170.934Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.237
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Convergent strategies in biosynthesis.
Dairi et al. (2011)
1 more

1 mention without citation

HMP binding protein ThiY and HMP-P synthase THI5 are structural homologues.
Bale et al. (2010)