1vnc: Difference between revisions
New page: left|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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[[Image:1vnc.gif|left|200px]]<br /><applet load="1vnc" size=" | [[Image:1vnc.gif|left|200px]]<br /><applet load="1vnc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vnc, resolution 2.1Å" /> | caption="1vnc, resolution 2.1Å" /> | ||
'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''<br /> | '''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''<br /> | ||
==Overview== | ==Overview== | ||
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis | 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== | ==About this Structure== | ||
1VNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Curvularia_inaequalis Curvularia inaequalis] with VO4 and AZI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1VNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Curvularia_inaequalis Curvularia inaequalis] with <scene name='pdbligand=VO4:'>VO4</scene> and <scene name='pdbligand=AZI:'>AZI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VNC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: vanadium-containing haloperoxidase]] | [[Category: vanadium-containing haloperoxidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:57 2008'' | ||
Revision as of 16:36, 21 February 2008
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CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS
OverviewOverview
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 StructureAbout this Structure
1VNC is a Single protein structure of sequence from Curvularia inaequalis with and as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Full crystallographic information is available from OCA.
ReferenceReference
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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