3FE5

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

3FE5 の概要

• エントリーDOI: 10.2210/pdb3fe5/pdb
• 関連するPDBエントリー: 1YFY 1ZVF 2QNK
• 分子名称: 3-hydroxyanthranilate 3,4-dioxygenase, FE (III) ION (3 entities in total)
• 機能のキーワード: cupin, 3hao, quinolinic acid, cytoplasm, dioxygenase, iron, metal-binding, oxidoreductase
• 由来する生物種: Bos taurus (Bovine)
• 細胞内の位置: Cytoplasm : Q0VCA8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32504.72

構造登録者

Dilovic, I.,Gliubich, F.,Malpeli, G.,Zanotti, G.,Matkovic-Calogovic, D. (登録日: 2008-11-27, 公開日: 2009-06-09, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.51 Å)