4a71: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==cytochrome c peroxidase in complex with phenol== | ==cytochrome c peroxidase in complex with phenol== | ||
<StructureSection load='4a71' size='340' side='right' caption='[[4a71]], [[Resolution|resolution]] 1.61Å' scene=''> | <StructureSection load='4a71' size='340' side='right'caption='[[4a71]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a71]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A71 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</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=4a71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a71 OCA], [https://pdbe.org/4a71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a71 RCSB], [https://www.ebi.ac.uk/pdbsum/4a71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a71 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Metcalfe | [[Category: Metcalfe CL]] | ||
[[Category: Moody | [[Category: Moody PCE]] | ||
[[Category: Murphy | [[Category: Murphy EJ]] | ||
[[Category: Raven | [[Category: Raven EL]] | ||
Latest revision as of 14:20, 20 December 2023
cytochrome c peroxidase in complex with phenolcytochrome c peroxidase in complex with phenol
Structural highlights
FunctionCCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMedGuaiacol is a universal substrate for all peroxidases, and its use in a simple colorimetric assay has wide applications. However, its exact binding location has never been defined. Here we report the crystal structures of guaiacol bound to cytochrome c peroxidase (CcP). A related structure with phenol bound is also presented. The CcP-guaiacol and CcP-phenol crystal structures show that both guaiacol and phenol bind at sites distinct from the cytochrome c binding site and from the delta-heme edge, which is known to be the binding site for other substrates. Although neither guaiacol nor phenol is seen bound at the delta-heme edge in the crystal structures, inhibition data and mutagenesis strongly suggest that the catalytic binding site for aromatic compounds is the delta-heme edge in CcP. The functional implications of these observations are discussed in terms of our existing understanding of substrate binding in peroxidases [Gumiero A et al. (2010) Arch Biochem Biophys 500, 13-20]. Crystal structure of guaiacol and phenol bound to a heme peroxidase.,Murphy EJ, Metcalfe CL, Nnamchi C, Moody PC, Raven EL FEBS J. 2012 May;279(9):1632-9. doi: 10.1111/j.1742-4658.2011.08425.x. Epub 2011 , Dec 5. PMID:22093282[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||