3M46

The crystal structure of the D73A mutant of glycoside HYDROLASE (FAMILY 31) from Ruminococcus obeum ATCC 29174

3M46 の概要

• エントリーDOI: 10.2210/pdb3m46/pdb
• 関連するPDBエントリー: 3FFJ
• 分子名称: Uncharacterized protein, GLYCEROL (3 entities in total)
• 機能のキーワード: glycoside hydrolase (family 31), structural genomics, psi-2, protein structure initiative, mcsg, midwest center for structural genomics, hydrolase
• 由来する生物種: Ruminococcus obeum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 154903.00

構造登録者

Tan, K.,Tesar, C.,Freeman, L.,Babnigg, G.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-03-10, 公開日: 2010-03-23, 最終更新日: 2023-09-06)

主引用文献

Tan, K.,Tesar, C.,Wilton, R.,Keigher, L.,Babnigg, G.,Joachimiak, A.
Novel alpha-glucosidase from human gut microbiome: substrate specificities and their switch
Faseb J., 24:3939-3949, 2010

PubMed Abstract: The human intestine harbors a large number of microbes forming a complex microbial community that greatly affects the physiology and pathology of the host. In the human gut microbiome, the enrichment in certain protein gene families appears to be widespread. They include enzymes involved in carbohydrate metabolism such as glucoside hydrolases of dietary polysaccharides and glycoconjugates. We report the crystal structures (wild type, 2 mutants, and a mutant/substrate complex) and the enzymatic activity of a recombinant α-glucosidase from human gut bacterium Ruminococcus obeum. The first ever protein structures from this bacterium reveal a structural homologue to human intestinal maltase-glucoamylase with a highly conserved catalytic domain and reduced auxiliary domains. The α-glucosidase, a member of GH31 family, shows substrate preference for α(1-6) over α(1-4) glycosidic linkages and produces glucose from isomaltose as well as maltose. The preference can be switched by a single mutation at its active site, suggestive of widespread adaptation to utilization of a variety of polysaccharides by intestinal micro-organisms as energy resources.

PubMed: 20581222
DOI: 10.1096/fj.10-156257

実験手法

X-RAY DIFFRACTION (2.66 Å)