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5NBO

Bacteroides ovatus mixed linkage glucan PUL (MLGUL) GH16

Summary for 5NBO
Entry DOI10.2210/pdb5nbo/pdb
DescriptorGlycosyl hydrolase family 16, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsglycoside hydrolase, gh16, hydrolase
Biological sourceBacteroides ovatus
Total number of polymer chains2
Total formula weight61428.09
Authors
Hemsworth, G.R.,Tamura, K.,Dejean, G.,Rogers, T.E.,Pudlo, N.A.,Urs, K.,Jain, N.,Martens, E.C.,Brumer, H.,Davies, G.J. (deposition date: 2017-03-02, release date: 2017-10-25, Last modification date: 2024-01-17)
Primary citationTamura, K.,Hemsworth, G.R.,Dejean, G.,Rogers, T.E.,Pudlo, N.A.,Urs, K.,Jain, N.,Davies, G.J.,Martens, E.C.,Brumer, H.
Molecular Mechanism by which Prominent Human Gut Bacteroidetes Utilize Mixed-Linkage Beta-Glucans, Major Health-Promoting Cereal Polysaccharides.
Cell Rep, 21:417-430, 2017
Cited by
PubMed Abstract: Microbial utilization of complex polysaccharides is a major driving force in shaping the composition of the human gut microbiota. There is a growing appreciation that finely tuned polysaccharide utilization loci enable ubiquitous gut Bacteroidetes to thrive on the plethora of complex polysaccharides that constitute "dietary fiber." Mixed-linkage β(1,3)/β(1,4)-glucans (MLGs) are a key family of plant cell wall polysaccharides with recognized health benefits but whose mechanism of utilization has remained unclear. Here, we provide molecular insight into the function of an archetypal MLG utilization locus (MLGUL) through a combination of biochemistry, enzymology, structural biology, and microbiology. Comparative genomics coupled with growth studies demonstrated further that syntenic MLGULs serve as genetic markers for MLG catabolism across commensal gut bacteria. In turn, we surveyed human gut metagenomes to reveal that MLGULs are ubiquitous in human populations globally, which underscores the importance of gut microbial metabolism of MLG as a common cereal polysaccharide.
PubMed: 29020628
DOI: 10.1016/j.celrep.2017.09.049
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

226707

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