2dij: Difference between revisions

Crystals of the Y195F mutant of cyclodextrin glycosyltransferase from, Bacillus circulans strain 251 were subjected to a double soaking, procedure, in which they were first soaked in a solution containing the, inhibitor acarbose and subsequently in a solution containing maltohexaose., The refined structure of the resulting protein-carbohydrate complex has, final crystallographic and free R-factors for data in the 8-2.6 angstrom, resolution range of 15.0% and 21.5%, respectively, and reveals that a new, inhibitor, composed of nine saccharide residues, is bound in the active, site. The first four residues correspond to acarbose and occupy the same, subsites near the catalytic residues as observed in the previously, reported acarbose-enzyme complex [Strokopytov et al. (1995) Biochemistry, 34, 2234-2240]. An oliogosaccharide consisting of five glucose residues, has been coupled to the nonreducing end of acarbose. At the fifth residue, the polysaccharide chain makes a sharp turn, allowing it to interact with, residues Tyr89, Phe195, and Asn193 and a flexible loop formed by residues, 145-148. On the basis of the refined model of the complex an explanation, is given for the product specificity of CGTases.

2DIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with CA and ADH as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1DIJ. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Structure known Active Sites: 16, 26, 36, CA1, CA2 and CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DIJ OCA].  

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