› 3hx9

X-ray diffraction
1.75Å resolution

Structure of heme-degrader, MhuD (Rv3592), from Mycobacterium tuberculosis with two hemes bound in its active site

Released:
DOI: 10.2210/pdb3hx9/pdb
PDB entry 3hx9 coloured by chain, front view.
PDB entry 3hx9 coloured by chain, side view.
PDB entry 3hx9 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis.
Chim N, Iniguez A, Nguyen TQ, Goulding CW
J Mol Biol 395 595-608 (2010)
PMID: 19917297

Function and Biology Details

Reaction catalysed: 
Protoheme + 3 reduced acceptor + 3 O(2) = mycobilin a + Fe(2+) + 3 acceptor + 3 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-161743 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase (mycobilin-producing) Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.25 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WKH3 (Residues: 1-105; Coverage: 100%)
Gene names: Rv3592, mhuD
Sequence domains: Antibiotic biosynthesis monooxygenase
Structure domains: Alpha-Beta Plaits

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 43.971Å b: 64.622Å c: 71.082Å
α: 90° β: 90.01° γ: 90°
R-values:
R R work R free
0.189 0.186 0.231
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Nutritional immunity: transition metals at the pathogen-host interface.
Hood et al. (2012)
14 more

12 mentions without citation

The TB Structural Genomics Consortium: a decade of progress.
Chim et al. (2011)
11 more