2BUR

Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with 4-hydroxybenzoate

2BUR の概要

• エントリーDOI: 10.2210/pdb2bur/pdb
• 関連するPDBエントリー: 1EO2 1EO9 1EOA 1EOB 1EOC 2BUM 2BUQ 2BUT 2BUU 2BUV 2BUW 2BUX 2BUY 2BUZ 2BV0
• 分子名称: PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN, PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN, FE (III) ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, dioxygenase, aromatic degradation, non-heme iron, beta- sandwich, mixed alpha/beta structure
• 由来する生物種: ACINETOBACTER CALCOACETICUS; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51285.10

構造登録者

Vetting, M.W.,Valley, M.P.,D'Argenio, D.A.,Ornston, L.N.,Lipscomb, J.D.,Ohlendorf, D.H. (登録日: 2005-06-17, 公開日: 2006-09-05, 最終更新日: 2023-12-13)

主引用文献

Brown, C.K.,Vetting, M.W.,Earhart, C.A.,Ohlendorf, D.H.
Biophysical Analyses of Designed and Selected Mutants of Protocatechuate 3,4-Dioxygenase
Annu.Rev.Microbiol., 58:555-585, 2004

PubMed Abstract: The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

PubMed: 15487948
DOI: 10.1146/ANNUREV.MICRO.57.030502.090927

実験手法

X-RAY DIFFRACTION (1.8 Å)