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Cite: NAR/gkaa742 2020



PUL General Information

Literature Information

PUL ID

PUL0646

PubMed

33587952, J Biol Chem. 2021 Jan-Jun;296:100415. doi: 10.1016/j.jbc.2021.100415. Epub 2021 Feb 13.

Characterization method

recombinant protein expression,crystallization,affinity gel electrophoresis,isothermal titration calorimetry

Genomic accession number

NZ_GL882612.1

Nucelotide position range

2624-15125

Substrate

beta-glucan

Loci

HMPREF9446_RS02735-HMPREF9446_RS02760

Species

Bacteroides fluxus YIT 12057/626930

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

bglX HMPREF9446_RS02735 WP_009123870.1 0 - 2253 (-) NZ_GL882612.1:2624-4877 3.2.1.21
- HMPREF9446_RS02740 WP_039968351.1 2255 - 3548 (-) NZ_GL882612.1:4879-6172 -
- HMPREF9446_RS02745 WP_009123872.1 3687 - 4560 (-) NZ_GL882612.1:6311-7184 -
- HMPREF9446_RS02750 WP_009123873.1 4589 - 6122 (-) NZ_GL882612.1:7213-8746 -
- HMPREF9446_RS02755 WP_009123874.1 6143 - 9326 (-) NZ_GL882612.1:8767-11950 -
- HMPREF9446_RS02760 WP_039968353.1 9616 - 12502 (-) NZ_GL882612.1:12240-15126 -

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

bglX 1 - 2253 (-) CAZyme: GH3|GH3 Yes
- 2256 - 3548 (-) CAZyme: GH158| GH158|3.2.1.39 Yes
- 3688 - 4560 (-) other Yes
- 4590 - 6122 (-) other Yes
- 6144 - 9326 (-) TC: gnl|TC-DB|Q45780|1.B.14.6.1 Yes
- 9617 - 12502 (-) TF: DBD-Pfam|GerE No

PUL ID

PUL0646

PubMed

33587952, J Biol Chem. 2021 Jan-Jun;296:100415. doi: 10.1016/j.jbc.2021.100415. Epub 2021 Feb 13.

Title

Distinct protein architectures mediate species-specific beta-glucan binding and metabolism in the human gut microbiota.

Author

Tamura K, Dejean G, Van Petegem F, Brumer H

Abstract

Complex glycans that evade our digestive system are major nutrients that feed the human gut microbiota (HGM). The prevalence of Bacteroidetes in the HGM of populations worldwide is engendered by the evolution of polysaccharide utilization loci (PULs), which encode concerted protein systems to utilize the myriad complex glycans in our diets. Despite their crucial roles in glycan recognition and transport, cell-surface glycan-binding proteins (SGBPs) remained understudied cogs in the PUL machinery. Here, we report the structural and biochemical characterization of a suite of SGBP-A and SGBP-B structures from three syntenic beta(1,3)-glucan utilization loci (1,3GULs) from Bacteroides thetaiotaomicron (Bt), Bacteroides uniformis (Bu), and B. fluxus (Bf), which have varying specificities for distinct beta-glucans. Ligand complexes provide definitive insight into beta(1,3)-glucan selectivity in the HGM, including structural features enabling dual beta(1,3)-glucan/mixed-linkage beta(1,3)/beta(1,4)-glucan-binding capability in some orthologs. The tertiary structural conservation of SusD-like SGBPs-A is juxtaposed with the diverse architectures and binding modes of the SGBPs-B. Specifically, the structures of the trimodular BtSGBP-B and BuSGBP-B revealed a tandem repeat of carbohydrate-binding module-like domains connected by long linkers. In contrast, BfSGBP-B comprises a bimodular architecture with a distinct beta-barrel domain at the C terminus that bears a shallow binding canyon. The molecular insights obtained here contribute to our fundamental understanding of HGM function, which in turn may inform tailored microbial intervention therapies.