3MO4

The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697

3MO4 の概要

• エントリーDOI: 10.2210/pdb3mo4/pdb
• 分子名称: Alpha-1,3/4-fucosidase, TYROSINE, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase
• 由来する生物種: Bifidobacterium longum subsp. infantis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107721.35

構造登録者

Tan, K.,Xu, X.,Cui, H.,Ng, J.,Savchenko, A.,Edwards, A.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-04-22, 公開日: 2010-05-12, 最終更新日: 2024-10-16)

主引用文献

Sela, D.A.,Garrido, D.,Lerno, L.,Wu, S.,Tan, K.,Eom, H.J.,Joachimiak, A.,Lebrilla, C.B.,Mills, D.A.
Bifidobacterium longum subsp. infantis ATCC 15697 alpha-fucosidases are active on fucosylated human milk oligosaccharides.
Appl.Environ.Microbiol., 78:795-803, 2012

PubMed Abstract: Bifidobacterium longum subsp. infantis ATCC 15697 utilizes several small-mass neutral human milk oligosaccharides (HMOs), several of which are fucosylated. Whereas previous studies focused on endpoint consumption, a temporal glycan consumption profile revealed a time-dependent effect. Specifically, among preferred HMOs, tetraose was favored early in fermentation, with other oligosaccharides consumed slightly later. In order to utilize fucosylated oligosaccharides, ATCC 15697 possesses several fucosidases, implicating GH29 and GH95 α-L-fucosidases in a gene cluster dedicated to HMO metabolism. Evaluation of the biochemical kinetics demonstrated that ATCC 15697 expresses three fucosidases with a high turnover rate. Moreover, several ATCC 15697 fucosidases are active on the linkages inherent to the HMO molecule. Finally, the HMO cluster GH29 α-L-fucosidase possesses a crystal structure that is similar to previously characterized fucosidases.

PubMed: 22138995
DOI: 10.1128/AEM.06762-11

実験手法

X-RAY DIFFRACTION (1.901 Å)