| Structural highlights
4a78 is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | 1a2f, 1a2g, 1aa4, 1ac4, 1ac8, 1aeb, 1aed, 1aee, 1aef, 1aeg, 1aeh, 1aej, 1aek, 1aem, 1aen, 1aeo, 1aeq, 1aes, 1aet, 1aeu, 1aev, 1bej, 1bek, 1bem, 1bep, 1beq, 1bes, 1bj9, 1bva, 1cca, 1ccb, 1ccc, 1cce, 1ccg, 1cci, 1ccj, 1cck, 1ccl, 1ccp, 1cmp, 1cmq, 1cmt, 1cmu, 1cpd, 1cpe, 1cpf, 1cpg, 1cyf, 1dcc, 1dj1, 1dj5, 1ds4, 1dse, 1dsg, 1dso, 1dsp, 1ebe, 1jci, 1jdr, 1kok, 1krj, 1kxm, 1kxn, 1mk8, 1mkq, 1mkr, 1ml2, 1ryc, 1s6v, 1sdq, 1sog, 1stq, 1u74, 1u75, 1z53, 1zby, 1zbz, 2b0z, 2b10, 2b11, 2b12, 2bcn, 2ccp, 2cep, 2cyp, 2gb8, 2pcb, 2pcc, 2v23, 2v2e, 2x07, 2x08, 2xil, 2xj5, 2xj8, 2y5a, 2ycg, 3ccp, 3ccx, 4a6z, 4a71, 4a7m, 4ccp, 4ccx, 5ccp, 6ccp, 7ccp |
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
References
- ↑ 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
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