5M1I
Structure of GH36 alpha-galactosidase from Thermotoga maritima in a covalent complex with a cyclopropyl carbasugar.
Summary for 5M1I
| Entry DOI | 10.2210/pdb5m1i/pdb |
| Descriptor | Alpha-galactosidase, SULFATE ION, (1~{R},2~{S},3~{S},4~{S},6~{R})-4-fluoranyl-1-(hydroxymethyl)bicyclo[4.1.0]heptane-2,3-diol, ... (5 entities in total) |
| Functional Keywords | alpha-galactosidase, glycoside hydrolase, hydrolase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 1 |
| Total formula weight | 67695.47 |
| Authors | Pengelly, R.,Gloster, T. (deposition date: 2016-10-07, release date: 2016-11-09, Last modification date: 2024-11-13) |
| Primary citation | Adamson, C.,Pengelly, R.J.,Shamsi Kazem Abadi, S.,Chakladar, S.,Draper, J.,Britton, R.,Gloster, T.M.,Bennet, A.J. Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars. Angew.Chem.Int.Ed.Engl., 55:14978-14982, 2016 Cited by PubMed Abstract: Glycoside hydrolases (GHs) have attracted considerable attention as targets for therapeutic agents, and thus mechanism-based inhibitors are of great interest. We report the first structural analysis of a carbocyclic mechanism-based GH inactivator, the results of which show that the two Michaelis complexes are in H conformations. We also report the synthesis and reactivity of a fluorinated analogue and the structure of its covalently linked intermediate (flattened H half-chair). We conclude that these inactivator reactions mainly involve motion of the pseudo-anomeric carbon atom, knowledge that should stimulate the design of new transition-state analogues for use as chemical biology tools. PubMed: 27783466DOI: 10.1002/anie.201607431 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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