1EW6

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

Summary for 1EW6

• Entry DOI: 10.2210/pdb1ew6/pdb
• Related: 1EWA
• Descriptor: DEHALOPEROXIDASE, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: globin, halophenols, oxidoreductase
• Biological source: Amphitrite ornata
• Total number of polymer chains: 2
• Total formula weight: 32522.29

Authors

Lebioda, L. (deposition date: 2000-04-24, release date: 2000-05-10, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.78 Å)