1aeu

From Proteopedia

Revision as of 13:41, 5 November 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

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