2015年12月21日
Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from Listeria innocua.
FEBS letters
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- 巻
- 589
- 号
- 24 Pt B
- 開始ページ
- 3816
- 終了ページ
- 21
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.febslet.2015.11.034
Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for β-mannosides. Here, we characterized β-1,2-mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with β-1,2-linked mannooligosaccharides. β-1,2-Mannotriose was bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open-close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided.
- リンク情報
- ID情報
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- DOI : 10.1016/j.febslet.2015.11.034
- PubMed ID : 26632508