5T9X

Crystal structure of BuGH16Bwt

5T9X の概要

• エントリーDOI: 10.2210/pdb5t9x/pdb
• 関連するPDBエントリー: 5T98 5T99 5T9A 5T9G 5TA0 5TA1 5TA5 5TA7 5TA9
• 分子名称: Glycoside Hydrolase, SODIUM ION, IMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: (alpha/beta)6 barrel, glycoside hydrolase, hydrolase
• 由来する生物種: Bacteroides uniformis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 117633.10

構造登録者

Pluvinage, B.,Boraston, A.B. (登録日: 2016-09-09, 公開日: 2017-09-13, 最終更新日: 2023-10-04)

主引用文献

Pluvinage, B.,Grondin, J.M.,Amundsen, C.,Klassen, L.,Moote, P.E.,Xiao, Y.,Thomas, D.,Pudlo, N.A.,Anele, A.,Martens, E.C.,Inglis, G.D.,Uwiera, R.E.R.,Boraston, A.B.,Abbott, D.W.
Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont.
Nat Commun, 9:1043-1043, 2018

PubMed Abstract: In red algae, the most abundant principal cell wall polysaccharides are mixed galactan agars, of which agarose is a common component. While bioconversion of agarose is predominantly catalyzed by bacteria that live in the oceans, agarases have been discovered in microorganisms that inhabit diverse terrestrial ecosystems, including human intestines. Here we comprehensively define the structure-function relationship of the agarolytic pathway from the human intestinal bacterium Bacteroides uniformis (Bu) NP1. Using recombinant agarases from Bu NP1 to completely depolymerize agarose, we demonstrate that a non-agarolytic Bu strain can grow on GAL released from agarose. This relationship underscores that rare nutrient utilization by intestinal bacteria is facilitated by the acquisition of highly specific enzymes that unlock inaccessible carbohydrate resources contained within unusual polysaccharides. Intriguingly, the agarolytic pathway is differentially distributed throughout geographically distinct human microbiomes, reflecting a complex historical context for agarose consumption by human beings.

PubMed: 29535379
DOI: 10.1038/s41467-018-03366-x

実験手法

X-RAY DIFFRACTION (2.5 Å)