3IXF

Crystal Structure of Dehaloperoxidase B at 1.58 and Structural Characterization of the AB Dimer from Amphitrite ornata

Summary for 3IXF

• Entry DOI: 10.2210/pdb3ixf/pdb
• Descriptor: Dehaloperoxidase B, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• Functional Keywords: peroxidase, globin, heme, oxygen transport, transport, oxidoreductase
• Biological source: Amphitrite ornata
• Total number of polymer chains: 2
• Total formula weight: 32574.21

Authors

de Serrano, V.S.,D'Antonio, J.,Thompson, M.K.,Franzen, S.,Ghiladi, R.A. (deposition date: 2009-09-03, release date: 2010-05-19, Last modification date: 2023-09-06)

Primary citation

de Serrano, V.,D'Antonio, J.,Franzen, S.,Ghiladi, R.A.
Structure of dehaloperoxidase B at 1.58 A resolution and structural characterization of the AB dimer from Amphitrite ornata.
Acta Crystallogr.,Sect.D, 66:529-538, 2010

PubMed Abstract: As members of the globin superfamily, dehaloperoxidase (DHP) isoenzymes A and B from the marine annelid Amphitrite ornata possess hemoglobin function, but they also exhibit a biologically relevant peroxidase activity that is capable of converting 2,4,6-trihalophenols to the corresponding 2,6-dihaloquinones in the presence of hydrogen peroxide. Here, a comprehensive structural study of recombinant DHP B, both by itself and cocrystallized with isoenzyme A, using X-ray diffraction is presented. The structure of DHP B refined to 1.58 A resolution exhibits the same distal histidine (His55) conformational flexibility as that observed in isoenzyme A, as well as additional changes to the distal and proximal hydrogen-bonding networks. Furthermore, preliminary characterization of the DHP AB heterodimer is presented, which exhibits differences in the AB interface that are not observed in the A-only or B-only homodimers. These structural investigations of DHP B provide insights that may relate to the mechanistic details of the H(2)O(2)-dependent oxidative dehalogenation reaction catalyzed by dehaloperoxidase, present a clearer description of the function of specific residues in DHP at the molecular level and lead to a better understanding of the paradigms of globin structure-function relationships.

PubMed: 20445228
DOI: 10.1107/S0907444910004580

Experimental method

X-RAY DIFFRACTION (1.58 Å)