3CTT
Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine
Summary for 3CTT
| Entry DOI | 10.2210/pdb3ctt/pdb |
| Related | 2qly 2qmj |
| Descriptor | Maltase-glucoamylase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | glycosyl hydrolase family 31, alpha-glucosidase, glycoprotein, glycosidase, membrane, multifunctional enzyme, signal-anchor, sulfation, transmembrane, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Apical cell membrane; Single-pass type II membrane protein: O43451 |
| Total number of polymer chains | 1 |
| Total formula weight | 100158.52 |
| Authors | Sim, L.,Rose, D.R. (deposition date: 2008-04-14, release date: 2009-02-24, Last modification date: 2024-10-30) |
| Primary citation | Cardona, F.,Parmeggiani, C.,Faggi, E.,Bonaccini, C.,Gratteri, P.,Sim, L.,Gloster, T.M.,Roberts, S.,Davies, G.J.,Rose, D.R.,Goti, A. Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families Chemistry, 15:1627-1636, 2009 Cited by PubMed Abstract: Total synthesis of naturally occurring casuarine (1) and the first total synthesis of casuarine 6-O-alpha-glucoside (2) were achieved through complete stereoselective nitrone cycloaddition, Tamao-Fleming oxidation and selective alpha-glucosylation as key steps. Biological assays of the two compounds proved their strong and selective inhibitory properties towards glucoamylase NtMGAM and trehalase Tre37A, respectively, which place them among the most powerful inhibitors of these enzymes. The structural determination of the complexes of NtMGAM with 1 and of Tre37A with 2 revealed interesting similarities in the catalytic sites of these two enzymes which belong to different families and clans. PubMed: 19123216DOI: 10.1002/chem.200801578 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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