2vhd: Difference between revisions

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-[[Image:2vhd.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2vhd", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2vhd|  PDB=2vhd  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PSEUDOMONAS AERUGINOSA- MIXED VALENCE FORM'''
+==Crystal Structure Of The Di-Haem Cytochrome C Peroxidase From Pseudomonas aeruginosa - Mixed Valence Form==
+<StructureSection load='2vhd' size='340' side='right'caption='[[2vhd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2vhd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VHD 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]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=2vhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhd OCA], [https://pdbe.org/2vhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vhd RCSB], [https://www.ebi.ac.uk/pdbsum/2vhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vhd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCPR_PSEAE CCPR_PSEAE] Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
+== 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/vh/2vhd_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=2vhd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A recombinant form of the prototypic diheme bacterial cytochrome c peroxidase (BCCP) from Pseudomonas aeruginosa (PsaCCP) has been expressed in Escherichia coli and purified to homogeneity. This material was used to carry out the first integrated biochemical, spectroscopic and structural investigation of the factors leading to reductive activation of this class of enzymes. A single, tightly bound, Ca2+ ion (K = 3 x 1010 M-1) found at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity. Reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis. The enzyme also forms a mixed-valence state in the absence of Ca2+ ions, but a combination of electronic absorption, and EPR spectroscopies suggests that under these circumstances the low potential heme remains six-coordinate, unable to bind substrate and therefore catalytically inactive. Our observations strongly suggest that the two mixed-valence forms of native PsaCCP reported previously by Foote and colleagues (Foote, N., Peterson, J., Gadsby, P., Greenwood, C., and Thomson, A. (1985) Biochem. J. 230, 227-237) correspond to the Ca2+-loaded and -depleted forms of the enzyme.
-==Overview==
+Redox-Linked Structural Changes Associated with the Formation of a Catalytically Competent Form of the Diheme Cytochrome c Peroxidase from Pseudomonas aeruginosa(,).,Echalier A, Brittain T, Wright J, Boycheva S, Mortuza GB, Fulop V, Watmough NJ Biochemistry. 2008 Feb 19;47(7):1947-1956. Epub 2008 Jan 25. PMID:18217775<ref>PMID:18217775</ref>
-A recombinant form of the prototypic diheme bacterial cytochrome c peroxidase (BCCP) from Pseudomonas aeruginosa (PsaCCP) has been expressed in Escherichia coli and purified to homogeneity. This material was used to carry out the first integrated biochemical, spectroscopic and structural investigation of the factors leading to reductive activation of this class of enzymes. A single, tightly bound, Ca2+ ion (K = 3 x 1010 M-1) found at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity. Reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis. The enzyme also forms a mixed-valence state in the absence of Ca2+ ions, but a combination of electronic absorption, and EPR spectroscopies suggests that under these circumstances the low potential heme remains six-coordinate, unable to bind substrate and therefore catalytically inactive. Our observations strongly suggest that the two mixed-valence forms of native PsaCCP reported previously by Foote and colleagues (Foote, N., Peterson, J., Gadsby, P., Greenwood, C., and Thomson, A. (1985) Biochem. J. 230, 227-237) correspond to the Ca2+-loaded and -depleted forms of the enzyme.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-VHD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHD OCA].
+</div>
+<div class="pdbe-citations 2vhd" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Redox-Linked Structural Changes Associated with the Formation of a Catalytically Competent Form of the Diheme Cytochrome c Peroxidase from Pseudomonas aeruginosa(,)., Echalier A, Brittain T, Wright J, Boycheva S, Mortuza GB, Fulop V, Watmough NJ, Biochemistry. 2008 Feb 19;47(7):1947-1956. Epub 2008 Jan 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18217775 18217775]
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
-[[Category: Cytochrome-c peroxidase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pseudomonas aeruginosa]]
-[[Category: Single protein]]
+[[Category: Boycheva S]]
-[[Category: Boycheva, S.]]
+[[Category: Brittain T]]
-[[Category: Brittain, T.]]
+[[Category: Echalier A]]
-[[Category: Echalier, A.]]
+[[Category: Fulop V]]
-[[Category: Fulop, V.]]
+[[Category: Mortuza GB]]
-[[Category: Mortuza, G B.]]
+[[Category: Watmough NJ]]
-[[Category: Watmough, N J.]]
+[[Category: Wright J]]
-[[Category: Wright, J.]]
-[[Category: Electron transport]]
-[[Category: Heme]]
-[[Category: Iron]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Periplasm]]
-[[Category: Peroxidase]]
-[[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:48:31 2008''