6CA1
THE CRYSTAL STRUCTURE OF THE W169Y MUTANT OF ALPHA-GLUCOSIDASE (GH 31) FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with miglitol
Summary for 6CA1
| Entry DOI | 10.2210/pdb6ca1/pdb |
| Descriptor | Glycosyl hydrolase, family 31, (2R,3R,4R,5S)-1-(2-hydroxyethyl)-2-(hydroxymethyl)piperidine-3,4,5-triol, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | structural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase |
| Biological source | Blautia obeum ATCC 29174 |
| Total number of polymer chains | 2 |
| Total formula weight | 155497.56 |
| Authors | Tan, K.,Tesar, C.,Jedrzejczak, R.,Joachimiak, A.,Midwest Center for Macromolecular Research (MCMR),Midwest Center for Structural Genomics (MCSG) (deposition date: 2018-01-29, release date: 2018-02-28, Last modification date: 2026-09-30) |
| Primary citation | Tan, K.,Tesar, C.,Wilton, R.,Jedrzejczak, R.P.,Joachimiak, A. Interaction of antidiabetic alpha-glucosidase inhibitors and gut bacteria alpha-glucosidase. Protein Sci., 27:1498-1508, 2018 Cited by PubMed Abstract: Carbohydrate hydrolyzing α-glucosidases are commonly found in microorganisms present in the human intestine microbiome. We have previously reported crystal structures of an α-glucosidase from the human gut bacterium Blaubia (Ruminococcus) obeum (Ro-αG1) and its substrate preference/specificity switch. This novel member of the GH31 family is a structural homolog of human intestinal maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) with a highly conserved active site that is predicted to be common in Ro-αG1 homologs among other species that colonize the human gut. In this report, we present structures of Ro-αG1 in complex with the antidiabetic α-glucosidase inhibitors voglibose, miglitol, and acarbose and supporting binding data. The in vitro binding of these antidiabetic drugs to Ro-αG1 suggests the potential for unintended in vivo crossreaction of the α-glucosidase inhibitors to bacterial α-glucosidases that are present in gut microorganism communities. Moreover, analysis of these drug-bound enzyme structures could benefit further antidiabetic drug development. PubMed: 29761590DOI: 10.1002/pro.3444 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
