5m12 | pdb_00005m12

Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with intact cyclopropyl-carbasugar.

spinqualitylabelsall models 5m12, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m12 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 7D0, MG, SO4 Activity: Alpha-galactosidase, with EC number 3.2.1.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 2 H3 conformations. We also report the synthesis and reactivity of a fluorinated analogue and the structure of its covalently linked intermediate (flattened 2 H3 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. Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars.,Adamson C, Pengelly RJ, Shamsi Kazem Abadi S, Chakladar S, Draper J, Britton R, Gloster TM, Bennet AJ Angew Chem Int Ed Engl. 2016 Nov 21;55(48):14978-14982. doi:, 10.1002/anie.201607431. Epub 2016 Oct 26. PMID:27783466 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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