› 4adm

X-ray diffraction
1.65Å resolution

Crystal structure of Rv1098c in complex with meso-tartrate

Released:
DOI: 10.2210/pdb4adm/pdb
PDB entry 4adm coloured by chain, front view.
PDB entry 4adm coloured by chain, side view.
PDB entry 4adm coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis.
Mechaly AE, Haouz A, Miras I, Barilone N, Weber P, Shepard W, Alzari PM, Bellinzoni M
FEBS Lett 586 1606-11 (2012)
PMID: 22561013

Function and Biology Details

Reaction catalysed: 
(S)-malate = fumarate + 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-161839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarate hydratase class II Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 495 amino acids
Theoretical weight: 52.72 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WN93 (Residues: 1-473; Coverage: 100%)
Gene names: MTV017.51c, Rv1098c, fum, fumC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand SRT 2 x SRT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 188.94Å b: 96.49Å c: 139.65Å
α: 90° β: 112.44° γ: 90°
R-values:
R R work R free
0.164 0.163 0.185
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Priming ammonia lyases and aminomutases for industrial and therapeutic applications.
Heberling et al. (2013)
1 more

1 mention without citation

The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.
Yan et al. (2022)