› 1i4n

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1i4n/pdb
PDB entry 1i4n coloured by chain, front view.
PDB entry 1i4n coloured by chain, side view.
PDB entry 1i4n coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges.
Knöchel T, Pappenberger A, Jansonius JN, Kirschner K
J Biol Chem 277 8626-34 (2002)
PMID: 11741953

Function and Biology Details

Reaction catalysed: 
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indole-3-glycerol phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 28.57 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56319 (Residues: 2-252; Coverage: 100%)
Gene names: TM_0140, trpC
Sequence domains: Indole-3-glycerol phosphate synthase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P43
Unit cell:
a: 48.93Å b: 48.93Å c: 248.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.233
Expression system: Escherichia coli

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Citations

1 review citation

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
8 other articles

6 mentions without citation

De novo enzyme design using Rosetta3.
Richter et al. (2011)
5 more