1AEU

SPECIFICITY OF LIGAND BINDING IN A POLAR CAVITY OF CYTOCHROME C PEROXIDASE (2-METHYLIMIDAZOLE)

Summary for 1AEU

• Entry DOI: 10.2210/pdb1aeu/pdb
• Descriptor: CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, 2-METHYLIMIDAZOLE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, peroxidase, transit peptide
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion matrix: P00431
• Total number of polymer chains: 1
• Total formula weight: 34157.83

Authors

Musah, R.A.,Jensen, G.M.,Fitzgerald, M.M.,Mcree, D.E.,Goodin, D.B. (deposition date: 1997-02-25, release date: 1997-09-04, Last modification date: 2024-05-22)

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

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: 8673607
DOI: 10.1038/nsb0796-626

Experimental method

X-RAY DIFFRACTION (2.1 Å)