1dy4: Difference between revisions
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Revision as of 15:57, 30 October 2007
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CBH1 IN COMPLEX WITH S-PROPRANOLOL
OverviewOverview
Cellobiohydrolase Cel7A (previously called CBH 1), the major cellulase, produced by the mould fungus Trichoderma reesei, has been successfully, exploited as a chiral selector for separation of stereo-isomers of some, important pharmaceutical compounds, e.g. adrenergic beta-blockers., Previous investigations, including experiments with catalytically, deficient mutants of Cel7A, point unanimously to the active site as being, responsible for discrimination of enantiomers.In this work the structural, basis for enantioselectivity of basic drugs by Cel7A has been studied by, X-ray crystallography. The catalytic domain of Cel7A was co-crystallised, with the (S)-enantiomer of a common beta-blocker, propranolol, at pH 7, and the structure of the complex was determined and refined at 1. 9 A, ... [(full description)]
About this StructureAbout this Structure
1DY4 is a [Single protein] structure of sequence from [Hypocrea jecorina] with NAG, CO and SNP as [ligands]. Active as [Cellulose 1,4-beta-cellobiosidase], with EC number [3.2.1.91]. Structure known Active Sites: CAT and COB. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for enantiomer binding and separation of a common beta-blocker: crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 A resolution., Stahlberg J, Henriksson H, Divne C, Isaksson R, Pettersson G, Johansson G, Jones TA, J Mol Biol. 2001 Jan 5;305(1):79-93. PMID:11114249
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