3m4f

Publication Abstract from PubMed

In this study, the crystal structure of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9A 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.

Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum.,Michaux C, Pouyez J, Mayard A, Vandurm P, Housen I, Wouters J Biochimie. 2010 Jul 16. PMID:20621155^[1]

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