› 1v7y

X-ray diffraction
2.5Å resolution

Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature

Released:
DOI: 10.2210/pdb1v7y/pdb
PDB entry 1v7y coloured by chain, front view.
PDB entry 1v7y coloured by chain, side view.
PDB entry 1v7y coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone.
Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K
Biochemistry 44 1184-92 (2005)
PMID: 15667212

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 domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-141673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A877 (Residues: 1-268; Coverage: 100%)
Gene names: JW1252, b1260, trpA
Sequence domains: Tryptophan synthase alpha chain
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: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 158.42Å b: 45.1Å c: 72.06Å
α: 90° β: 96.9° γ: 90°
R-values:
R R work R free
0.218 0.218 0.271
Expression system: Escherichia coli

Quick links

Citations

14 citation in other articles

Increasing protein stability by improving beta-turns.
Fu et al. (2009)
13 more

3 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
2 more