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Publication Abstract from PubMed

Thermostable enzymes employ various structural features dictated at the amino-acid sequence level that allow them to maintain their integrity at higher temperatures. Many hypotheses as to the nature of thermal stability have been proposed, including optimized core hydrophobicity and an increase in charged surface residues to enhance polar solvent interactions for solubility. Here, the three-dimensional structure of the family GH11 xylanase from the moderate thermophile Thermobifida fusca in its trapped covalent glycosyl-enzyme intermediate complex is presented. Interactions with the bound ligand show fewer direct hydrogen bonds from ligand to protein than observed in previous complexes from other species and imply that binding of the xylan substrate involves several water-mediated hydrogen bonds.

Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca.,van Bueren AL, Otani S, Friis EP, Wilson KS, Davies GJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):141-4. Epub, 2012 Jan 25. PMID:22297985^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.