2cxg

From Proteopedia

Revision as of 15:09, 30 October 2007

CYCLODEXTRIN GLYCOSYLTRANSFERASE COMPLEXED TO THE INHIBITOR ACARBOSE

Overview

Crystals of cyclodextrin glycosyltransferase (CGTase) from Bacillus, circulans strain 251 were soaked in buffer solutions containing the, pseudotetrasaccharide acarbose, a strong amylase- and CGTase inhibitor., The X-ray structure of the complex was elucidated at 2.5-A resolution with, a final crystallographic R value of 15.8% for all data between 8.0 and 2.5, A. Acarbose is bound near the catalytic residues Asp229, Glu257, and, Asp328. The carboxylic group of Glu257 is at hydrogen bonding distance, from the glycosidic oxygen in the scissile bond between the B and C sugars, (residue A is at the nonreducing end of the inhibitor). Asp328 makes, hydrogen bonds with the 4-amino-4,6-dideoxyglucose (residue B), and Asp229, is in a close van der Waals contact with the C1 atom of this sugar. ... [(full description)]

About this Structure

2CXG is a [Single protein] structure of sequence from [Bacillus circulans] with CA as [ligand]. This structure superseeds the now removed PDB entry 1CXG. Active as [Cyclomaltodextrin glucanotransferase], with EC number [2.4.1.19]. Structure known Active Sites: CA1, CA2, CAT, MB1, MB2 and MB3. Full crystallographic information is available from [OCA].

Reference

X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases., Strokopytov B, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW, Biochemistry. 1995 Feb 21;34(7):2234-40. PMID:7857935

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