› 2bet

X-ray diffraction
2.2Å resolution

Structure of Mycobacterium tuberculosis Ribose-5-Phosphate Isomerase, RpiB, Rv2465c, in complex with 4-phospho-D-erythronate.

Released:
DOI: 10.2210/pdb2bet/pdb
PDB entry 2bet coloured by chain, front view.
PDB entry 2bet coloured by chain, side view.
PDB entry 2bet coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism.
Roos AK, Burgos E, Ericsson DJ, Salmon L, Mowbray SL
J Biol Chem 280 6416-22 (2005)
PMID: 15590681

Function and Biology Details

Reaction catalysed: 
D-ribose 5-phosphate = D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-5-phosphate isomerase B Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 172 amino acids
Theoretical weight: 18.47 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P9WKD7 (Residues: 1-162; Coverage: 100%)
Gene names: MTV008.21c, Rv2465c, rpiB
Sequence domains: Ribose/Galactose Isomerase
Structure domains: Sugar-phosphate isomerase, RpiB/LacA/LacB

Ligands and Environments

1 bound ligand:
Ligand DEZ 5 x DEZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 136.735Å b: 102.71Å c: 69.988Å
α: 90° β: 95.85° γ: 90°
R-values:
R R work R free
0.214 0.212 0.25
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Lipoarabinomannan and related glycoconjugates: structure, biogenesis and role in Mycobacterium tuberculosis physiology and host-pathogen interaction.
Mishra et al. (2011)
3 more

2 mentions without citation

Relating destabilizing regions to known functional sites in proteins.
Dessailly et al. (2007)
1 more