Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca

TY - JOUR

T1 - Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca

AU - van Bueren, Alicia Lammerts

AU - Otani, Suzie

AU - Friis, Esben P.

AU - Wilson, Keith S.

AU - Davies, Gideon J.

PY - 2012/2

Y1 - 2012/2

N2 - 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.

AB - 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.

KW - GLYCOSYL-ENZYME INTERMEDIATE

KW - DIRECTED EVOLUTION

KW - CRYSTALLOGRAPHY

KW - xylanases

KW - THERMAL-STABILITY

KW - MOLECULAR-GRAPHICS

KW - HYDROLYSIS

KW - CONFORMATION

KW - PROTEINS

KW - covalent intermediate

KW - thermostability

KW - glycoside hydrolases

KW - BETA-1,4-XYLANASES

KW - COMPLEXES

UR - http://www.scopus.com/inward/record.url?scp=84856852121&partnerID=8YFLogxK

U2 - 10.1107/S1744309111049608

DO - 10.1107/S1744309111049608

M3 - Article

SN - 1744-3091

VL - 68

SP - 141

EP - 144

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 2

ER -