1qhb
From Proteopedia
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VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS
Overview
The three-dimensional structure of the vanadium bromoperoxidase protein, from the marine red macroalgae Corallina officinalis has been determined, by single isomorphous replacement at 2.3 A resolution. The enzyme subunit, is made up of 595 amino acid residues folded into a single alpha+beta, domain. There are 12 bromoperoxidase subunits, arranged with 23-point, group symmetry. A cavity is formed by the N terminus of each subunit in, the centre of the dodecamer. The subunit fold and dimer organisation of, the Cor. officinalis vanadium bromoperoxidase are similar to those of the, dimeric enzyme from the brown algae Ascophyllum nodosum, with which it, shares 33 % sequence identity. The different oligomeric state of the two, algal enzymes seems to reflect separate mechanisms of adaptation to harsh, environmental conditions and/or to chemically active substrates and, products. The residues involved in the vanadate binding are conserved, between the two algal bromoperoxidases and the vanadium chloroperoxidase, from the fungus Curvularia inaequalis. However, most of the other residues, forming the active-site cavity are different in the three enzymes, which, reflects differences in the substrate specificity and stereoselectivity of, the reaction. A dimer of the Cor. officinalis enzyme partially, superimposes with the two-domain monomer of the fungal enzyme.
About this Structure
1QHB is a Single protein structure of sequence from Corallina officinalis with PO4 and CA as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Full crystallographic information is available from OCA.
Reference
Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis., Isupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN, Littlechild JA, J Mol Biol. 2000 Jun 16;299(4):1035-49. PMID:10843856
Page seeded by OCA on Sun Nov 25 04:06:18 2007
