› 3daq

X-ray diffraction
1.45Å resolution

Crystal structure of dihydrodipicolinate synthase from methicillin-resistant Staphylococcus aureus

Released:
DOI: 10.2210/pdb3daq/pdb
PDB entry 3daq coloured by chain, front view.
PDB entry 3daq coloured by chain, side view.
PDB entry 3daq coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Primary publication:
Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen.
Burgess BR, Dobson RCJ, Bailey MF, Atkinson SC, Griffin MDW, Jameson GB, Parker MW, Gerrard JA, Perugini MA
J Biol Chem 283 27598-27603 (2008)
PMID: 18684709

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179667 (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: 292 amino acids
Theoretical weight: 32.14 KDa
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GH13 (Residues: 2-293; Coverage: 99%)
Gene names: SAR1407, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand CL 4 x CL
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P1
Unit cell:
a: 65.41Å b: 67.573Å c: 77.998Å
α: 90.13° β: 68.85° γ: 72.29°
R-values:
R R work R free
0.134 0.132 0.161
Expression system: Escherichia coli

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Citations

1 review citation

The role of quaternary structure in (beta/alpha)(8)-barrel proteins: evolutionary happenstance or a higher level of structure-function relationships?
Devenish et al. (2009)
43 other articles

3 mentions without citation

Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.
Soares da Costa et al. (2018)
2 more