› 2kzh

Solution NMR

Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from Escherichia coli

Released:
DOI: 10.2210/pdb2kzh/pdb
PDB entry 2kzh coloured by chain, ensemble of 20 models, front view.
PDB entry 2kzh coloured by chain, ensemble of 20 models, side view.
PDB entry 2kzh coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (βα)8 barrel fold.
Setiyaputra S, Mackay JP, Patrick WM
J Mol Biol 408 291-303 (2011)
PMID: 21354426

Function and Biology Details

Reactions catalysed: 
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan biosynthesis protein TrpCF Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.14 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00909 (Residues: 255-387; Coverage: 29%)
Gene names: JW1254, b1262, trpC, trpF
Sequence domains: N-(5'phosphoribosyl)anthranilate (PRA) isomerase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Rapid bursts and slow declines: on the possible evolutionary trajectories of enzymes.
Newton et al. (2015)
2 more