PDBsum entry: 1qhb

Oxidoreductase

PDB id: 1qhb

Contents

Protein chains

(+ 0 more) 595 a.a. *

Ligands

PO4 ×6

Metals

_CA ×6

Waters ×2186

* Residue conservation analysis

PDB id:

1qhb

Name:

Oxidoreductase

Title:

Vanadium bromoperoxidase from red alga corallina officinalis

Structure:

Haloperoxidase. Chain: a, b, c, d, e, f. Ec: 1.11.1.10

Source:

Corallina officinalis. Organism_taxid: 35170

Biol. unit:

Dodecamer (from PDB file)

Resolution:

2.30Å R-factor: 0.172 R-free: 0.227

Authors:

M.N.Isupov,A.R.Dalby,A.A.Brindley,J.A.Littlechild

Key ref:

M.N.Isupov et al. (2000). Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis. J Mol Biol, 299, 1035-1049. PubMed id: 10843856 DOI: 10.1006/jmbi.2000.3806

Date:

11-May-99 Release date: 05-Jul-00

Protein chains

Q8LLW7  (PRXV_COROI) -  Vanadium-dependent bromoperoxidase

Seq: 598 a.a.

Struc: 595 a.a.*

* PDB and UniProt seqs differ at 51 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.11.1.18 - Bromide peroxidase.
• Reaction: RH + HBr + H₂O₂ = RBr + 2 H₂O

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (1 term)
• Biological process: oxidation-reduction process (1 term)
• Biochemical function: catalytic activity (4 terms)

Added reference

DOI no: 10.1006/jmbi.2000.3806

J Mol Biol 299:1035-1049 (2000)

PubMed id: 10843856

Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.

M.N.Isupov, A.R.Dalby, A.A.Brindley, Y.Izumi, T.Tanabe, G.N.Murshudov, J.A.Littlechild.

ABSTRACT

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.

Selected figure(s)

Figure 3.
Figure 3. Structure of the CVBPO subunit. (a) A stereo view of the C^a trace. Each 20th residue is numbered. (b) Ribbon diagram of the subunit in the same orientation as in (a). a-Helices are numbered from 1 to 19. The inorganic phosphate ion bound at the vanadium site and the bound Mg2+ are shown as CPK space-filling models.

Figure 7.
Figure 7. The active site of the CVBPO enzyme. (a) The 2F[o] -F[c] electron density contoured at 1s is shown around the vanadate binding site occupied by the inorganic phosphate group (PO4). (b) A stereo ribbon diagram of the active site viewed from the outside. The phosphate ion is shown as a ball and stick model. Amino acid residues surrounding this site are shown as filled bonds. (c) The electrostatic potential surface of the CVBPO dimer viewed as in Figure 4(b). Positive charge is shown in blue and negative charge in red. The large active-site cleft can be seen on the right-hand side of the Figure. The drawing was prepared using the program GRASP [Nicholls et al 1991].

The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 299, 1035-1049) copyright 2000.

Figures were selected by an automated process.