1ac4
From Proteopedia
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VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)
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
1AC4 is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and TMT as [ligands]. Active as [[1]], with EC number [1.11.1.5]. 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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