4a6z | pdb_00004a6z

Cytochrome c peroxidase with bound guaiacol

spinqualitylabelsall models 4a6z, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a6z 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: HEM, JZ3 Related: 1cpg, 1bva, 2v23, 3ccx, 6ccp, 1aeu, 1dcc, 1s6v, 1bej, 1ml2, 1ccl, 1beq, 1jci, 1aem, 1u74, 2b10, 2pcc, 1aeb, 1ccg, 1cpd, 1cca, 1ac4, 2y5a, 1cmu, 1aeo, 1bep, 1aet, 1aev, 2pcb, 1aeh, 1kxn, 1aen, 1aeg, 5ccp, 4ccp, 2x07, 2cep, 1cmp, 1cce, 1ryc, 2xj8, 2b0z, 1bes, 1dsp, 1z53, 2b12, 1bem, 1mkr, 1ccj, 1sog, 1aee, 1cpe, 1a2f, 1jdr, 1dse, 1aes, 1a2g, 1zbz, 1bek, 1mkq, 1cck, 1mk8, 1ebe, 1cci, 1krj, 2b11, 1aef, 1cyf, 1aek, 1ccb, 1u75, 1ac8, 1dj1, 1dsg, 1dj5, 2ccp, 1cmt, 1aeq, 1ds4, 7ccp, 1aej, 1sdq, 2x08, 2gb8, 1kxm, 4ccx, 2xj5, 1bj9, 1kok, 2bcn, 1ccp, 1zby, 2cyp, 2ycg, 3ccp, 1stq, 1dso, 2v2e, 2xil, 1aa4, 1aed, 1cmq, 1ccc, 1cpf, 4a71 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c peroxidase

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