5TA1

Crystal structure of BuGH86wt

Summary for 5TA1

• Entry DOI: 10.2210/pdb5ta1/pdb
• Related: 5T98 5T99 5T9A 5T9G 5T9X 5TA0 5TA5 5TA7 5TA9
• Descriptor: Glycoside Hydrolase, CALCIUM ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: (alpha/beta)6 barrel, glycoside hydrolase, hydrolase
• Biological source: Bacteroides uniformis
• Total number of polymer chains: 1
• Total formula weight: 75333.41

Authors

Pluvinage, B.,Boraston, A.B. (deposition date: 2016-09-09, release date: 2017-09-13, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)