2JKE
Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with deoxynojirimycin
Summary for 2JKE
| Entry DOI | 10.2210/pdb2jke/pdb |
| Related | 2JKA 2JKP |
| Descriptor | ALPHA-GLUCOSIDASE (ALPHA-GLUCOSIDASE SUSB), 1-DEOXYNOJIRIMYCIN, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, glycoside hydrolase, family 97, alpha-glucosidase, bacteroides thetaiotaomicron, deoxynojirimycin |
| Biological source | BACTEROIDES THETAIOTAOMICRON |
| Total number of polymer chains | 2 |
| Total formula weight | 167517.62 |
| Authors | Gloster, T.M.,Turkenburg, J.P.,Potts, J.R.,Henrissat, B.,Davies, G.J. (deposition date: 2008-08-28, release date: 2008-09-30, Last modification date: 2023-12-13) |
| Primary citation | Gloster, T.M.,Turkenburg, J.P.,Potts, J.R.,Henrissat, B.,Davies, G.J. Divergence of Catalytic Mechanism within a Glycosidase Family Provides Insight Into Evolution of Carbohydrate Metabolism by Human Gut Flora. Chem.Biol., 15:1058-, 2008 Cited by PubMed Abstract: Enzymatic cleavage of the glycosidic bond yields products in which the anomeric configuration is either retained or inverted. Each mechanism reflects the dispositions of the enzyme functional groups; a facet of which is essentially conserved in 113 glycoside hydrolase (GH) families. We show that family GH97 has diverged significantly, as it contains both inverting and retaining alpha-glycosidases. This reflects evolution of the active center; a glutamate acts as a general base in inverting members, exemplified by Bacteroides thetaiotaomicron alpha-glucosidase BtGH97a, whereas an aspartate likely acts as a nucleophile in retaining members. The structure of BtGH97a and its complexes with inhibitors, coupled to kinetic analysis of active-site variants, reveals an unusual calcium ion dependence. 1H NMR analysis shows an inversion mechanism for BtGH97a, whereas another GH97 enzyme from B. thetaiotaomicron, BtGH97b, functions as a retaining alpha-galactosidase. PubMed: 18848471DOI: 10.1016/J.CHEMBIOL.2008.09.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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