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| | <StructureSection load='2vhd' size='340' side='right'caption='[[2vhd]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2vhd' size='340' side='right'caption='[[2vhd]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vhd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. 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> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eb7|1eb7]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></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> | | <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> | | </table> |
| | == Function == | | == 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.
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cytochrome-c peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boycheva, S]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Brittain, T]] | + | [[Category: Boycheva S]] |
| - | [[Category: Echalier, A]] | + | [[Category: Brittain T]] |
| - | [[Category: Fulop, V]] | + | [[Category: Echalier A]] |
| - | [[Category: Mortuza, G B]] | + | [[Category: Fulop V]] |
| - | [[Category: Watmough, N J]] | + | [[Category: Mortuza GB]] |
| - | [[Category: Wright, J]] | + | [[Category: Watmough NJ]] |
| - | [[Category: Electron transport]]
| + | [[Category: Wright J]] |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
CCPR_PSEAE Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Echalier A, Brittain T, Wright J, Boycheva S, Mortuza GB, Fulop V, Watmough NJ. Redox-Linked Structural Changes Associated with the Formation of a Catalytically Competent Form of the Diheme Cytochrome c Peroxidase from Pseudomonas aeruginosa(,). Biochemistry. 2008 Feb 19;47(7):1947-1956. Epub 2008 Jan 25. PMID:18217775 doi:10.1021/bi702064f
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