5M1I

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

5M1I の概要

• エントリーDOI: 10.2210/pdb5m1i/pdb
• 分子名称: 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)
• 機能のキーワード: alpha-galactosidase, glycoside hydrolase, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67695.47

構造登録者

Pengelly, R.,Gloster, T. (登録日: 2016-10-07, 公開日: 2016-11-09, 最終更新日: 2024-11-13)

主引用文献

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

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: 27783466
DOI: 10.1002/anie.201607431

実験手法

X-RAY DIFFRACTION (1.55 Å)