期刊
BIOCHIMIE
卷 92, 期 10, 页码 1407-1415出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2010.07.003
关键词
Family 11 endoxylanase; pH adaptation; Crystal structure; Acidophilic; Structure/function relationship
资金
- Belgian National Fund for Scientific Research
In this study, the crystal structure of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9 angstrom resolution. This is one of the few solved crystal structures of acidophilic proteins. The enzyme has the overall fold typical to family 11 xylanases. Comparison of this structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases provides additional insights into the general features involved in low pH adaptation (stability and activity). Several sequence and structure modifications appeared to be responsible for the acidophilic characteristic: (a) the presence of an aspartic acid H bonded to the acid/base catalyst (b) the nature of specifically conserved residues in the active site (c) the negative potential at the surface (d) the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes. (C) 2010 Elsevier Masson SAS. All rights reserved.
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