1EW6

THE CRYSTAL STRUCTURE AND AMINO ACID SEQUENCE OF DEHALOPEROXIDASE FROM AMPHITRITE ORNATA INDICATE COMMON ANCESTRY WITH GLOBINS

1EW6 の概要

• エントリーDOI: 10.2210/pdb1ew6/pdb
• 関連するPDBエントリー: 1EWA
• 分子名称: DEHALOPEROXIDASE, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: globin, halophenols, oxidoreductase
• 由来する生物種: Amphitrite ornata
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32522.29

構造登録者

Lebioda, L. (登録日: 2000-04-24, 公開日: 2000-05-10, 最終更新日: 2024-02-07)

主引用文献

LaCount, M.W.,Zhang, E.,Chen, Y.P.,Han, K.,Whitton, M.M.,Lincoln, D.E.,Woodin, S.A.,Lebioda, L.
The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins.
J.Biol.Chem., 275:18712-18716, 2000

PubMed Abstract: The full-length, protein coding sequence for dehaloperoxidase was obtained using a reverse genetic approach and a cDNA library from marine worm Amphitrite ornata. The crystal structure of the dehaloperoxidase (DHP) was determined by the multiple isomorphous replacement method and was refined at 1.8-A resolution. The enzyme fold is that of the globin family and, together with the amino acid sequence information, indicates that the enzyme evolved from an ancient oxygen carrier. The peroxidase activity of DHP arose mainly through changes in the positions of the proximal and distal histidines relative to those seen in globins. The structure of a complex of DHP with 4-iodophenol is also reported, and it shows that in contrast to larger heme peroxidases DHP binds organic substrates in the distal cavity. The binding is facilitated by the histidine swinging in and out of the cavity. The modeled position of the oxygen atom bound to the heme suggests that the enzymatic reaction proceeds via direct attack of the oxygen atom on the carbon atom bound to the halogen atom.

PubMed: 10751397
DOI: 10.1074/jbc.M001194200

実験手法

X-RAY DIFFRACTION (1.78 Å)