4A78
cytochrome c peroxidase M119W in complex with guiacol
Summary for 4A78
| Entry DOI | 10.2210/pdb4a78/pdb |
| 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 |
| Descriptor | CYTOCHROME C PEROXIDASE, MITOCHONDRIAL, PROTOPORPHYRIN IX CONTAINING FE, Guaiacol, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, transit peptide, hydrogen peroxide, iron, heme, isoniazid, mitochondrion, metal-binding |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Mitochondrion matrix: P00431 |
| Total number of polymer chains | 1 |
| Total formula weight | 34535.16 |
| Authors | Murphy, E.J.,Metcalfe, C.L.,Raven, E.L.,Moody, P.C.E. (deposition date: 2011-11-11, release date: 2012-11-07, Last modification date: 2023-12-20) |
| Primary citation | Murphy, E.J.,Metcalfe, C.L.,Nnamchi, C.,Moody, P.C.E.,Raven, E.L. Crystal Structure of Guaiacol and Phenol Bound to a Heme Peroxidase. FEBS J., 279:1632-, 2012 Cited by PubMed Abstract: 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 δ-heme edge, which is known to be the binding site for other substrates. Although neither guaiacol nor phenol is seen bound at the δ-heme edge in the crystal structures, inhibition data and mutagenesis strongly suggest that the catalytic binding site for aromatic compounds is the δ-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]. PubMed: 22093282DOI: 10.1111/J.1742-4658.2011.08425.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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