1vnc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:46, 14 February 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1vnc.gif|left|200px]]
 
-
<!--
+
==CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS==
-
The line below this paragraph, containing "STRUCTURE_1vnc", creates the "Structure Box" on the page.
+
<StructureSection load='1vnc' size='340' side='right'caption='[[1vnc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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>
-
{{STRUCTURE_1vnc| PDB=1vnc | SCENE= }}
+
<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/initialview01.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>
-
'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''
+
==See Also==
-
 
+
*[[Haloperoxidase|Haloperoxidase]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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 [http://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].
+
-
 
+
-
==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:[http://www.ncbi.nlm.nih.gov/pubmed/8552646 8552646]
+
-
[[Category: Chloride peroxidase]]
+
[[Category: Curvularia inaequalis]]
[[Category: Curvularia inaequalis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Messerschmidt, A.]]
+
[[Category: Messerschmidt A]]
-
[[Category: Wever, R.]]
+
[[Category: Wever R]]
-
[[Category: Oxidoreductase]]
+
-
[[Category: Vanadium-containing haloperoxidase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:43:44 2008''
+

Current revision

CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS

PDB ID 1vnc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools