1h46
From Proteopedia
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THE CATALYTIC MODULE OF CEL7D FROM PHANEROCHAETE CHRYSOSPORIUM AS A CHIRAL SELECTOR: STRUCTURAL STUDIES OF ITS COMPLEX WITH THE B-BLOCKER (R)-PROPRANOLOL
Overview
Previous investigations have shown that the major cellobiohydrolase of, Phanerochaete chrysosporium, Cel7D (CBH 58), can be used to separate the, enantiomers of a number of drugs, including adrenergic beta blockers such, as propranolol. The structural basis of this enantioselectivity is, explored here. A 1.5 A X-ray structure of the catalytic domain of Cel7D in, complex with (R)-propranolol showed the ligand bound at the active site in, glucosyl-binding subsites -1/+1. The catalytic residue Glu207 makes a, strong charge-charge interaction with the secondary amine of, (R)-propranolol; this is supported by a second interaction of the amine, with the nearby Asp209. The aromatic naphthyl group stacks onto the indole, ring of Trp373 (normally the glucosyl-binding platform of subsite +1)., ... [(full description)]
About this Structure
1H46 is a [Single protein] structure of sequence from [Phanerochaete chrysosporium] with NAG and RNP as [ligands]. Active as [Cellulose 1,4-beta-cellobiosidase], with EC number [3.2.1.91]. Structure known Active Site: NAG. Full crystallographic information is available from [OCA].
Reference
The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:12657782
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