3M4F

Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum

3M4F の概要

• エントリーDOI: 10.2210/pdb3m4f/pdb
• 分子名称: Endo-1,4-beta-xylanase, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total)
• 機能のキーワード: family 11 endoxylanase, acidophilic adaptation, structure/function relationship, glycosidase, hydrolase, xylan degradation
• 由来する生物種: Scytalidium acidophilum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88371.76

構造登録者

Michaux, C.,Wouters, J. (登録日: 2010-03-11, 公開日: 2010-07-28, 最終更新日: 2024-10-30)

主引用文献

Michaux, C.,Pouyez, J.,Mayard, A.,Vandurm, P.,Housen, I.,Wouters, J.
Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum
Biochimie, 92:1407-1415, 2010

PubMed Abstract: In this study, the crystal structure of a novel endo-1,4-β-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9Å 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.

PubMed: 20621155
DOI: 10.1016/j.biochi.2010.07.003

実験手法

X-RAY DIFFRACTION (1.89 Å)