1AEU: SPECIFICITY OF LIGAND BINDING IN A POLAR CAVITY OF CYTOCHROME C PEROXIDASE (2-METHYLIMIDAZOLE)

Citation:
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.
PDB ID: 1AEUDownload
MMDB ID: 55173
PDB Deposition Date: 1997/2/25
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 1AEU: monomeric; determined by author
Molecular Components in 1AEU
Label Count Molecule
Protein (1 molecule)
1
Cytochrome C Peroxidase(Gene symbol: CCP1)
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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