2ehh

X-ray diffraction
1.9Å resolution

Crystal structure of dihydrodipicolinate synthase from aquifex aeolicus

Released:
Source organism: Aquifex aeolicus
Entry authors: Kumarevel TS, Karthe P, Kuramitsu S, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, C, D, E
Molecule details ›
Chains: A, C, D, E
Length: 294 amino acids
Theoretical weight: 32.71 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67216 (Residues: 1-294; Coverage: 100%)
Gene names: aq_1143, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 61.321Å b: 146.953Å c: 97.877Å
α: 90° β: 109.35° γ: 90°
R-values:
R R work R free
0.21 0.21 0.23
Expression system: Escherichia coli