› 3vnd

X-ray diffraction
2.6Å resolution

Crystal structure of tryptophan synthase alpha-subunit from the psychrophile Shewanella frigidimarina K14-2

Released:
DOI: 10.2210/pdb3vnd/pdb
PDB entry 3vnd coloured by chain, front view.
PDB entry 3vnd coloured by chain, side view.
PDB entry 3vnd coloured by chain, top view.
Source organism: Shewanella frigidimarina
Primary publication:
Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties.
Mitsuya D, Tanaka S, Matsumura H, Urano N, Takano K, Ogasahara K, Takehira M, Yutani K, Ishida M
J Biochem 155 73-82 (2014)
PMID: 24163283

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan synthase alpha chain Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 267 amino acids
Theoretical weight: 27.83 KDa
Source organism: Shewanella frigidimarina
Expression system: Escherichia coli
UniProt:
  • Canonical: H1AFK5 (Residues: 1-267; Coverage: 100%)
Gene name: trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SO4 18 x SO4
Ligand PE8 4 x PE8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2221
Unit cell:
a: 181.136Å b: 182.779Å c: 181.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.211
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein folding at extreme temperatures: Current issues.
Feller G. (2018)
1 more

1 mention without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)