3FE5

Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney

Summary for 3FE5

• Entry DOI: 10.2210/pdb3fe5/pdb
• Related: 1YFY 1ZVF 2QNK
• Descriptor: 3-hydroxyanthranilate 3,4-dioxygenase, FE (III) ION (3 entities in total)
• Functional Keywords: cupin, 3hao, quinolinic acid, cytoplasm, dioxygenase, iron, metal-binding, oxidoreductase
• Biological source: Bos taurus (Bovine)
• Cellular location: Cytoplasm : Q0VCA8
• Total number of polymer chains: 1
• Total formula weight: 32504.72

Authors

Dilovic, I.,Gliubich, F.,Malpeli, G.,Zanotti, G.,Matkovic-Calogovic, D. (deposition date: 2008-11-27, release date: 2009-06-09, Last modification date: 2024-10-16)

Primary citation

Dilovic, I.,Gliubich, F.,Malpeli, G.,Zanotti, G.,Matkovic-Calogovic, D.
Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase.
Biopolymers, 2009

PubMed 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 A resolution. The enzyme, which crystallizes in the triclinic P1 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.

PubMed: 19226621
DOI: 10.1002/bip.21167

Experimental method

X-RAY DIFFRACTION (2.51 Å)