› 6am8

X-ray diffraction
1.83Å resolution

Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9 with Trp bound as E(Aex2)

Released:
DOI: 10.2210/pdb6am8/pdb
PDB entry 6am8 coloured by chain, front view.
PDB entry 6am8 coloured by chain, side view.
PDB entry 6am8 coloured by chain, top view.
Source organism: Pyrococcus furiosus DSM 3638
Primary publication:
Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.
Buller AR, van Roye P, Cahn JKB, Scheele RA, Herger M, Arnold FH
J Am Chem Soc 140 7256-7266 (2018)
PMID: 29712420

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186371 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tryptophan synthase beta chain 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 396 amino acids
Theoretical weight: 43.62 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8U093 (Residues: 1-388; Coverage: 100%)
Gene names: PF1706, trpB1
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
Tryptophan synthase beta chain 1 Chains: B, C
Molecule details ›
Chains: B, C
Length: 396 amino acids
Theoretical weight: 43.39 KDa
Source organism: Pyrococcus furiosus DSM 3638
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8U093 (Residues: 1-388; Coverage: 100%)
Gene names: PF1706, trpB1
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand TRP 3 x TRP
Ligand NA 4 x NA
Ligand PLT 2 x PLT
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P212121
Unit cell:
a: 82.233Å b: 106.036Å c: 158.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Conformational dynamics and enzyme evolution.
Petrović et al. (2018)
8 more

2 mentions without citation

Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.
Buller et al. (2018)
1 more