2CEQ

Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole

Summary for 2CEQ

• Entry DOI: 10.2210/pdb2ceq/pdb
• Related: 1GOW 1UWI 1UWQ 1UWR 1UWS 1UWT 1UWU 2CER
• Descriptor: BETA-GALACTOSIDASE, ACETATE ION, GLUCOIMIDAZOLE, ... (4 entities in total)
• Functional Keywords: archaeon, family 1, glycoside hydrolase, glucoimidazole, glycosidase, hydrolase
• Biological source: SULFOLOBUS SOLFATARICUS
• Total number of polymer chains: 2
• Total formula weight: 114216.41

Authors

Gloster, T.M.,Moracci, M.,Vasella, A.,Davies, G.J. (deposition date: 2006-02-10, release date: 2006-09-27, Last modification date: 2023-12-13)

Primary citation

Gloster, T.M.,Roberts, S.,Perugino, G.,Rossi, M.,Moracci, M.,Panday, N.,Terinek, M.,Vasella, A.,Davies, G.J.
Structural, Kinetic, and Thermodynamic Analysis of Glucoimidazole-Derived Glycosidase Inhibitors.
Biochemistry, 45:11879-, 2006

PubMed Abstract: Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound.

PubMed: 17002288
DOI: 10.1021/BI060973X

Experimental method

X-RAY DIFFRACTION (2.14 Å)