› 1yl6

X-ray diffraction
2.9Å resolution

crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) (crystal form B)

Released:
DOI: 10.2210/pdb1yl6/pdb
PDB entry 1yl6 coloured by chain, front view.
PDB entry 1yl6 coloured by chain, side view.
PDB entry 1yl6 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms.
Janowski R, Kefala G, Weiss MS
Acta Crystallogr D Biol Crystallogr 66 61-72 (2010)
PMID: 20057050

Function and Biology Details

Reaction catalysed: 
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 25.7 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WP23 (Residues: 2-245; Coverage: 100%)
Gene names: MTV002.38c, Rv2773c, dapB
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21212
Unit cell:
a: 87.13Å b: 89.46Å c: 77.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.199 0.257
Expression system: Escherichia coli

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Citations

1 review citation

Structure and function of Mycobacterium tuberculosis meso-diaminopimelic acid (DAP) biosynthetic enzymes.
Usha et al. (2012)
11 other articles

3 mentions without citation

Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .
Parsonage et al. (2010)
2 more