› 2dh5

X-ray diffraction
2.9Å resolution

Crystal structure of E. coli Holo-TrpB

Released:
DOI: 10.2210/pdb2dh5/pdb
PDB entry 2dh5 coloured by chain, front view.
PDB entry 2dh5 coloured by chain, side view.
PDB entry 2dh5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding.
Nishio K, Ogasahara K, Morimoto Y, Tsukihara T, Lee SJ, Yutani K
FEBS J 277 2157-70 (2010)
PMID: 20370823

Function and Biology Details

Reaction catalysed: 
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase beta chain Chain: A
Molecule details ›
Chain: A
Length: 397 amino acids
Theoretical weight: 43.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A879 (Residues: 1-397; Coverage: 100%)
Gene names: JW1253, b1261, trpB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
2 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P6522
Unit cell:
a: 172.516Å b: 172.516Å c: 82.587Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.244
Expression system: Escherichia coli

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Citations

1 review citation

Pyridoxal 5'-Phosphate-Dependent Enzymes at the Crossroads of Host-Microbe Tryptophan Metabolism.
Cellini et al. (2020)
4 other articles