1VBU

Crystal structure of native xylanase 10B from Thermotoga maritima

1VBU の概要

• エントリーDOI: 10.2210/pdb1vbu/pdb
• 関連するPDBエントリー: 1VBR
• 分子名称: endo-1,4-beta-xylanase B, SULFATE ION, ACETIC ACID, ... (5 entities in total)
• 機能のキーワード: xylanase 10b, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78042.27

構造登録者

Ihsanawati,Kumasaka, T.,Kaneko, T.,Nakamura, S.,Tanaka, N. (登録日: 2004-03-02, 公開日: 2005-06-28, 最終更新日: 2023-12-27)

主引用文献

Ihsanawati,Kumasaka, T.,Kaneko, T.,Morokuma, C.,Yatsunami, R.,Sato, T.,Nakamura, S.,Tanaka, N.
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8
Proteins, 61:999-1009, 2005

PubMed Abstract: The crystal structure of xylanase 10B from Thermotoga maritima MSB8 (TmxB), a hyperthermostable xylanase, has been solved in its native form and in complex with xylobiose or xylotriose at 1.8 A resolution. In order to gain insight into the substrate subsite and the molecular features for thermal stability, we compared TmxB with family 10 xylanase structures from nine microorganisms. As expected, TmxB folds into a (beta/alpha)8-barrel structure, which is common among the glycoside hydrolase family 10. The enzyme active site and the environment surrounding the xylooligosaccharide of TmxB are highly similar to those of family 10 xylanases. However, only two xylose moieties were found in its binding pocket from the TmxB-xylotriose complex structure. This finding suggests that TmxB could be a potential biocatalyst for the large-scale production of xylobiose. The result of structural analyses also indicated that TmxB possesses some additional features that account for its thermostability. In particular, clusters of aromatic residues together with a lack of exposed hydrophobic residues are characteristic of the TmxB structure. TmxB has also a significant number of ion pairs on the protein surface that are not found in other thermophilic family 10 xylanases.

PubMed: 16247799
DOI: 10.1002/prot.20700

実験手法

X-RAY DIFFRACTION (1.8 Å)