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1vnc
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(New page: 200px<br /><applet load="1vnc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vnc, resolution 2.1Å" /> '''CHLOROPEROXIDASE FROM...)
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Revision as of 02:50, 21 November 2007
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CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS
Overview
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis, belongs to a class of vanadium enzymes that oxidize halides in the, presence of hydrogen peroxide to the corresponding hypohalous acids. The, 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex, reveals the geometry of the catalytic vanadium center. Azide coordinates, directly to the metal center, resulting in a structure with azide, three, nonprotein oxygens, and a histidine as ligands. In the native state, vanadium will be bound as hydrogen vanadate(V) in a trigonal bipyramidal, coordination with the metal coordinated to three oxygens in the equatorial, plane, to the OH group at one apical position, and to the epsilon 2, nitrogen of a histidine at the other apical position. The protein fold is, mainly alpha-helical with two four-helix bundles as main structural motifs, and an overall structure different from other structures. The helices pack, together to a compact molecule, which explains the high stability of the, protein. An amino acid sequence comparison with vanadium-containing, bromoperoxidase from the seaweed Ascophyllum nodosum shows high, similarities in the regions of the metal binding site, with all hydrogen, vanadate(V) interacting residues conserved except for lysine-353, which is, an asparagine.
About this Structure
1VNC is a Single protein structure of sequence from Curvularia inaequalis with VO4 and AZI as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Full crystallographic information is available from OCA.
Reference
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis., Messerschmidt A, Wever R, Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):392-6. PMID:8552646
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