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Crystal structure of bovine 3‐hydroxyanthranilate 3,4‐dioxygenase
Author(s) -
Đilović Ivica,
Gliubich Francesca,
Malpeli Giorgio,
Zanotti Giuseppe,
MatkovićČalogović Dubravka
Publication year - 2009
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21167
Subject(s) - chemistry , dimer , monomer , histidine , crystallography , triclinic crystal system , stereochemistry , crystal structure , enzyme , biochemistry , organic chemistry , polymer
Abstract 3‐Hydroxyanthranilate 3,4‐dioxygenase, the enzyme that catalyzes the conversion of 3‐hydroxyanthranilate to quinolinic acid, has been extracted and purified from bovine kidney, crystallized and its structure determined at 2.5 Å resolution. The enzyme, which crystallizes in the triclinic P 1 space group, is a monomer, characterized by the so‐called cupin fold. The monomer of the bovine enzyme mimics the dimer present in lower species, such as bacteria and yeast, since it is composed of two domains: one of them is equivalent to one monomer, whilst the second domain corresponds to only a portion of it. The active site consists of an iron ion coordinated by two histidine residues, one glutamate and an external ligand, which has been interpreted as a solvent molecule. It is contained in the N‐terminal domain, whilst the function of the C‐terminal domain is possibly structural. The catalytic mechanism very likely has been conserved through all species, since the positions of all residues considered relevant for the reaction are present from bacteria to humans. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1189–1195, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com