1vnc: Difference between revisions
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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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== | ==CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS== | ||
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis | <StructureSection load='1vnc' size='340' side='right'caption='[[1vnc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1vnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Curvularia_inaequalis Curvularia inaequalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VNC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vnc OCA], [https://pdbe.org/1vnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vnc RCSB], [https://www.ebi.ac.uk/pdbsum/1vnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vnc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRXC_CURIN PRXC_CURIN] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vn/1vnc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vnc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:8552646</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 1vnc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Haloperoxidase|Haloperoxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Curvularia inaequalis]] | [[Category: Curvularia inaequalis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Messerschmidt | [[Category: Messerschmidt A]] | ||
[[Category: Wever | [[Category: Wever R]] | ||
Latest revision as of 07:21, 13 August 2026
CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS
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