1ewa | pdb_00001ewa
Dehaloperoxidase and 4-iodophenol
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Overview
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.
About this Structure
1EWA is a Single protein structure of sequence from Amphitrite ornata with SO4, HEM and IOL as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins., LaCount MW, Zhang E, Chen YP, Han K, Whitton MM, Lincoln DE, Woodin SA, Lebioda L, J Biol Chem. 2000 Jun 23;275(25):18712-6. PMID:10751397
Page seeded by OCA on Sat Nov 24 22:56:31 2007
