1Z53
The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase
Summary for 1Z53
| Entry DOI | 10.2210/pdb1z53/pdb |
| Related | 1KOK 2CYP |
| Descriptor | Cytochrome c peroxidase, mitochondrial, PROTOPORPHYRIN IX (3 entities in total) |
| Functional Keywords | ccp, heme peroxidase, iron-free protoporphyrin ix, trp cation radical, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Mitochondrion matrix: P00431 |
| Total number of polymer chains | 1 |
| Total formula weight | 34133.90 |
| Authors | Bhaskar, B.,Poulos, T.L. (deposition date: 2005-03-17, release date: 2005-06-21, Last modification date: 2024-04-03) |
| Primary citation | Bhaskar, B.,Poulos, T.L. The 1.13-A structure of iron-free cytochrome c peroxidase. J.Biol.Inorg.Chem., 10:425-430, 2005 Cited by PubMed Abstract: The iron-free cytochrome c peroxidase (CCP) crystal structure has been determined to 1.13 A and compared with the 1.2-A ferric-CCP structure. Quite unexpectedly, removal of the iron has no effect on porphyrin geometry and distortion, indicating that protein-porphyrin interactions and not iron coordination or formation of the axial His-Fe bond determines porphyrin conformation. However, there are changes in solvent structure in the distal pocket, which lead to changes in the distal His52 acid-base catalyst. The observed ability of His52 to move in response to small changes in solvent structure is very likely important for its role as a catalyst in assisting in the heterolytic fission of the peroxide O-O bond. PubMed: 15900441DOI: 10.1007/s00775-005-0654-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.13 Å) |
Structure validation
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