4a71: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a71 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a71 RCSB], [http://www.ebi.ac.uk/pdbsum/4a71 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a71 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a71 RCSB], [http://www.ebi.ac.uk/pdbsum/4a71 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 15:18, 25 December 2014

cytochrome c peroxidase in complex with phenolcytochrome c peroxidase in complex with phenol

Structural highlights

4a71 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Cytochrome-c peroxidase, with EC number 1.11.1.5
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Publication Abstract from PubMed

Guaiacol 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 Also

References

  1. Murphy EJ, Metcalfe CL, Nnamchi C, Moody PC, Raven EL. Crystal structure of guaiacol and phenol bound to a heme peroxidase. FEBS J. 2012 May;279(9):1632-9. doi: 10.1111/j.1742-4658.2011.08425.x. Epub 2011 , Dec 5. PMID:22093282 doi:http://dx.doi.org/10.1111/j.1742-4658.2011.08425.x

4a71, resolution 1.61Å

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