1RYC
CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE
Summary for 1RYC
| Entry DOI | 10.2210/pdb1ryc/pdb |
| Descriptor | CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, BENZIMIDAZOLE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Mitochondrion matrix: P00431 |
| Total number of polymer chains | 1 |
| Total formula weight | 34192.88 |
| Authors | Fitzgerald, M.M.,Musah, R.,Mcree, D.E.,Goodin, D.B. (deposition date: 1996-05-10, release date: 1996-11-08, Last modification date: 2024-02-14) |
| Primary citation | Fitzgerald, M.M.,Musah, R.A.,McRee, D.E.,Goodin, D.B. A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity. Nat.Struct.Biol., 3:626-631, 1996 Cited by PubMed Abstract: Conformational changes that gate the access of substrates or ligands to an active site are important features of enzyme function. In this report, we describe an unusual example of a structural rearrangement near a buried artificial cavity in cytochrome c peroxidase that occurs on binding protonated benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a large solvent-accessible channel for the entry of ligands to an otherwise inaccessible binding site. The trapping of this alternate conformational state provides a unique view of the extent to which protein dynamics can allow small molecule penetration into buried protein cavities. PubMed: 8673607DOI: 10.1038/nsb0796-626 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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