› 3ta6

X-ray diffraction
1.41Å resolution

Structure of Mycobacterium tuberculosis triosephosphate isomerase

Released:
DOI: 10.2210/pdb3ta6/pdb
PDB entry 3ta6 coloured by chain, front view.
PDB entry 3ta6 coloured by chain, side view.
PDB entry 3ta6 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural and functional characterization of Mycobacterium tuberculosis triosephosphate isomerase.
Connor SE, Capodagli GC, Deaton MK, Pegan SD
Acta Crystallogr D Biol Crystallogr 67 1017-22 (2011)
PMID: 22120738

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 28.26 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WG43 (Residues: 1-261; Coverage: 100%)
Gene names: MTCY493.16c, Rv1438, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2
Unit cell:
a: 134.917Å b: 52.589Å c: 77.539Å
α: 90° β: 104.48° γ: 90°
R-values:
R R work R free
0.132 0.131 0.155
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Triosephosphate isomerase is dispensable in vitro yet essential for Mycobacterium tuberculosis to establish infection.
Trujillo et al. (2014)
2 more

1 mention without citation

Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase.
Singhal et al. (2015)