1qhb | pdb_00001qhb

VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS

spinqualitylabelsall models 1qhb, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qhb is a 6 chain structure with sequence from Corallina officinalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, PO4 Activity: Chloride peroxidase, with EC number 1.11.1.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PRXV_COROI] Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Haloperoxidase

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