Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca.
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.
Structural Biology Laboratory, Department of Chemistry, University of York, York, England.
Alicia Lammerts
AL
van Bueren
Suzie
S
Otani
Esben P
EP
Friis
Keith S
KS
Wilson
Gideon J
GJ
Davies
D000192:Actinomycetales / Q000201:enzymology*; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
D043364:Endo-1,4-beta Xylanases