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Three-Dimensional Structure of a Thermophilic Family Gh11 Xylanase from Thermobifida Fusca

DOI: 10.1107/S1744309111049608 DOI Help
PMID: 22297985 PMID Help

Authors: Alicia Lammerts Van Bueren (Department of Biochemistry and Microbiology, University of Victoria) , Suzie Otani (Novozymes A/S) , Esben P. Friis (Novozymes A/S) , Keith S. Wilson (University of York) , Gideon J. Davies (University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 68 (2) , PAGES 141 - 144

State: Published (Approved)
Published: February 2012
Diamond Proposal Number(s): 1221

Abstract: 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.

Journal Keywords: Crystallography; X-Ray; Endo-1; Hydrogen; Models; Molecular; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Added On: 30/03/2012 13:27

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