› 3uwu

X-ray diffraction
2.15Å resolution

Crystal structure of Staphylococcus Aureus triosephosphate isomerase complexed with glycerol-3-phosphate

Released:
DOI: 10.2210/pdb3uwu/pdb
PDB entry 3uwu coloured by chain, front view.
PDB entry 3uwu coloured by chain, side view.
PDB entry 3uwu coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Primary publication:
Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop.
Mukherjee S, Roychowdhury A, Dutta D, Das AK
Biochimie 94 2532-44 (2012)
PMID: 22813930

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-179678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 28.26 KDa
Source organism: Staphylococcus aureus subsp. aureus MRSA252
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GIL6 (Residues: 1-253; Coverage: 100%)
Gene names: SAR0830, tpi, tpiA
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand G3P 2 x G3P
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 81.1Å b: 81.1Å c: 174.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.223
Expression system: Escherichia coli

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Citations

5 citation in other articles

Biochemical characterisation of triose phosphate isomerase from the liver fluke Fasciola hepatica.
Zinsser et al. (2013)
4 more

2 mentions without citation

Ancient Regulatory Role of Lysine Acetylation in Central Metabolism.
Nakayasu et al. (2017)
1 more