1vnc

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[[Image:1vnc.gif|left|200px]]
[[Image:1vnc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1vnc |SIZE=350|CAPTION= <scene name='initialview01'>1vnc</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1vnc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1vnc| PDB=1vnc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vnc OCA], [http://www.ebi.ac.uk/pdbsum/1vnc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vnc RCSB]</span>
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}}
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'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''
'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''
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[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt, A.]]
[[Category: Wever, R.]]
[[Category: Wever, R.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: vanadium-containing haloperoxidase]]
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[[Category: Vanadium-containing haloperoxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:43:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:26:29 2008''
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Revision as of 09:43, 3 May 2008

Image:1vnc.gif

Template:STRUCTURE 1vnc

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. 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 Page seeded by OCA on Sat May 3 12:43:44 2008

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