› 1r88

X-ray diffraction
1.71Å resolution

The crystal structure of Mycobacterium tuberculosis MPT51 (FbpC1)

Released:
DOI: 10.2210/pdb1r88/pdb
PDB entry 1r88 coloured by chain, front view.
PDB entry 1r88 coloured by chain, side view.
PDB entry 1r88 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic alpha/beta hydrolases.
Wilson RA, Maughan WN, Kremer L, Besra GS, Fütterer K
J Mol Biol 335 519-30 (2004)
PMID: 14672660

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MPT51/MPB51 antigen Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 29.46 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQN7 (Residues: 27-299; Coverage: 100%)
Gene names: MTV026.08c, Rv3803c, fbpC1, fbpD, mpb51, mpt51
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 59.9Å b: 108.9Å c: 109.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.205
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis.
Takayama et al. (2005)
4 more

2 mentions without citation

Identification of a mycoloyl transferase selectively involved in O-acylation of polypeptides in Corynebacteriales.
Huc et al. (2013)
1 more