The Crystal Structure and Amino Acid Sequence of Dehaloperoxidase from Amphitrite ornata Indicate Common Ancestry with Globins

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-...

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Bibliographic Details
Published in:The Journal of biological chemistry 2000-06, Vol.275 (25), p.18712-18716
Main Authors: LaCount, Michael W., Zhang, Erli, Chen, Yung Pin, Han, Kaiping, Whitton, Margaret M., Lincoln, David E., Woodin, Sarah A., Lebioda, Lukasz
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amphitrite ornata
Animals
Cloning, Molecular
Crystallography, X-Ray
dehaloperoxidase
Hemoglobins
Molecular Sequence Data
Peroxidases - chemistry
Peroxidases - genetics
Polychaeta - enzymology
Protein Conformation
Sequence Homology, Amino Acid
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Summary: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-Å 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M001194200