› 3pb0

X-ray diffraction
2Å resolution

Characterisation of the first monomeric dihydrodipicolinate synthase variant reveals evolutionary insights

Released:
DOI: 10.2210/pdb3pb0/pdb
PDB entry 3pb0 coloured by chain, front view.
PDB entry 3pb0 coloured by chain, side view.
PDB entry 3pb0 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization.
Pearce FG, Dobson RC, Jameson GB, Perugini MA, Gerrard JA
Biochim Biophys Acta 1814 1900-9 (2011)
PMID: 21803176

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 300 amino acids
Theoretical weight: 32.93 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1K9 (Residues: 1-294; Coverage: 100%)
Gene names: TM_1521, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 70.458Å b: 131.472Å c: 74.15Å
α: 90° β: 89.99° γ: 90°
R-values:
R R work R free
0.152 0.151 0.197
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Enhanced thermal stability and specific activity of Pseudomonas aeruginosa lipoxygenase by fusing with self-assembling amphipathic peptides.
Lu et al. (2013)
3 more