1ulv
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(New page: 200px<br /><applet load="1ulv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ulv, resolution 2.42Å" /> '''Crystal Structure of...)
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Revision as of 02:04, 25 November 2007
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Crystal Structure of Glucodextranase Complexed with Acarbose
Overview
A glucodextranase (iGDase) from Arthrobacter globiformis I42 hydrolyzes, alpha-1,6-glucosidic linkages of dextran from the non-reducing end to, produce beta-D-glucose via an inverting reaction mechanism and classified, into the glycoside hydrolase family 15 (GH15). Here we cloned the iGDase, gene and determined the crystal structures of iGDase of the unliganded, form and the complex with acarbose at 2.42-A resolution. The structure of, iGDase is composed of four domains N, A, B, and C. Domain A forms an, (alpha/alpha)(6)-barrel structure and domain N consists of 17 antiparallel, beta-strands, and both domains are conserved in bacterial glucoamylases, (GAs) and appear to be mainly concerned with catalytic activity. The, structure of iGDase complexed with acarbose revealed that the positions, and orientations of the residues at subsites -1 and +1 are nearly, identical between iGDase and GA; however, the residues corresponding to, subsite 3, which form the entrance of the substrate binding pocket, and, the position of the open space and constriction of iGDase are different, from those of GAs. On the other hand, domains B and C are not found in the, bacterial GAs. The primary structure of domain C is homologous with a, surface layer homology domain of pullulanases, and the three-dimensional, structure of domain C resembles the carbohydrate-binding domain of some, glycohydrolases.
About this Structure
1ULV is a Single protein structure of sequence from Arthrobacter globiformis with ACR and CA as ligands. Active as Glucan 1,6-alpha-glucosidase, with EC number 3.2.1.70 Full crystallographic information is available from OCA.
Reference
Structural insights into substrate specificity and function of glucodextranase., Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y, J Biol Chem. 2004 Mar 12;279(11):10575-83. Epub 2003 Dec 1. PMID:14660574
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