1H1A

Thermophilic beta-1,4-xylanase from Chaetomium thermophilum

1H1A の概要

• エントリーDOI: 10.2210/pdb1h1a/pdb
• 分子名称: Endo-1,4-beta-xylanase, UNKNOWN ATOM OR ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, xylanase, glycosyl hydrolase, family 11, thermostability glycosidase
• 由来する生物種: Chaetomium thermophilum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42505.72

構造登録者

Hakulinen, N.,Rouvinen, J. (登録日: 2002-07-05, 公開日: 2003-07-04, 最終更新日: 2024-11-06)

主引用文献

Hakulinen, N.,Turunen, O.,Janis, J.,Leisola, M.,Rouvinen, J.
Three-Dimensional Structures of Thermophilic Beta-1,4-Xylanases from Chaetomium Thermophilum and Nonomuraea Flexuosa. Comparison of Twelve Xylanases in Relation to Their Thermal Stability.
Eur.J.Biochem., 270:1399-1412, 2003

PubMed Abstract: The crystal structures of thermophilic xylanases from Chaetomium thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A resolution, respectively. Both enzymes have the overall fold typical to family 11 xylanases with two highly twisted beta-sheets forming a large cleft. The comparison of 12 crystal structures of family 11 xylanases from both mesophilic and thermophilic organisms showed that the structures of different xylanases are very similar. The sequence identity differences correlated well with the structural differences. Several minor modifications appeared to be responsible for the increased thermal stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased number of charged residues, especially Arg, resulting in enhanced polar interactions, and (c) improved stabilization of secondary structures involved the higher number of residues in the beta-strands and stabilization of the alpha-helix region. Some members of family 11 xylanases have a unique strategy to improve their stability, such as a higher number of ion pairs or aromatic residues on protein surface, a more compact structure, a tighter packing, and insertions at some regions resulting in enhanced interactions.

PubMed: 12653995
DOI: 10.1046/J.1432-1033.2003.03496.X

実験手法

X-RAY DIFFRACTION (1.75 Å)