› 3afe

X-ray diffraction
2.5Å resolution

Crystal structure of the HsaA monooxygenase from M.tuberculosis

Released:
DOI: 10.2210/pdb3afe/pdb
PDB entry 3afe coloured by chain, front view.
PDB entry 3afe coloured by chain, side view.
PDB entry 3afe coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism.
Dresen C, Lin LY, D'Angelo I, Tocheva EI, Strynadka N, Eltis LD
J Biol Chem 285 22264-75 (2010)
PMID: 20448045

Function and Biology Details

Reaction catalysed: 
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH(2) + O(2) = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent monooxygenase, oxygenase subunit HsaA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 394 amino acids
Theoretical weight: 43.19 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WJA1 (Residues: 1-394; Coverage: 100%)
Gene names: Rv3570c, hsaA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 90.968Å b: 94.009Å c: 98.094Å
α: 90° β: 93.94° γ: 90°
R-values:
R R work R free
0.194 0.191 0.258
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Microbial steroid transformations: current state and prospects.
Donova et al. (2012)
20 more

4 mentions without citation

A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism.
Dresen et al. (2010)
3 more