› 1uzl

X-ray diffraction
2Å resolution

MabA from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb1uzl/pdb
PDB entry 1uzl coloured by chain, front view.
PDB entry 1uzl coloured by chain, side view.
PDB entry 1uzl coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis.
Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A
J Mol Biol 320 249-61 (2002)
PMID: 12079383

Function and Biology Details

Reactions catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
(R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase MabA Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 25.73 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGT3 (Residues: 1-247; Coverage: 100%)
Gene names: MTCY277.04, Rv1483, fabG1, mabA
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand CS 4 x CS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 81.579Å b: 117.159Å c: 52.495Å
α: 90° β: 122.65° γ: 90°
R-values:
R R work R free
0.187 0.18 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
16 more

2 mentions without citation

Indel PDB: a database of structural insertions and deletions derived from sequence alignments of closely related proteins.
Hsing et al. (2008)
1 more