1ac8
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(New page: 200px<br /> <applet load="1ac8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ac8, resolution 2.1Å" /> '''VARIATION IN THE STR...)
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Revision as of 17:12, 29 October 2007
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VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)
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
1AC8 is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and TMZ 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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