1aeu

From Proteopedia

Revision as of 12:42, 30 October 2007

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

Overview

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.

About this Structure

1AEU is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and 2MZ as [ligands]. Active as [Cytochrome-c peroxidase], with EC number [1.11.1.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].

Reference

A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity., Fitzgerald MM, Musah RA, McRee DE, Goodin DB, Nat Struct Biol. 1996 Jul;3(7):626-31. PMID:8673607

Page seeded by OCA on Tue Oct 30 14:47:37 2007