› 1i7s

X-ray diffraction
2.4Å resolution

ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN

Released:
DOI: 10.2210/pdb1i7s/pdb
PDB entry 1i7s coloured by chain, front view.
PDB entry 1i7s coloured by chain, side view.
PDB entry 1i7s coloured by chain, top view.
Source organism: Serratia marcescens
Primary publication:
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE
Proc Natl Acad Sci U S A 98 6021-6 (2001)
PMID: 11371633

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Anthranilate synthase component 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 519 amino acids
Theoretical weight: 57.66 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00897 (Residues: 1-519; Coverage: 100%)
Gene name: trpE
Sequence domains:
Structure domains: Anthranilate synthase
Anthranilate synthase component 2 Chains: B, D
Molecule details ›
Chains: B, D
Length: 193 amino acids
Theoretical weight: 20.95 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00900 (Residues: 1-193; Coverage: 100%)
Gene name: trpG
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 72.271Å b: 123.561Å c: 179.646Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.318
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Conformational changes in ammonia-channeling glutamine amidotransferases.
Mouilleron et al. (2007)
6 more

10 mentions without citation

A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.
Parthasarathy et al. (2018)
9 more