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Bacteroides thetaiotaomicron generates diverse α-mannosidase activities through subtle evolution of a distal substrate-binding motif.

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Thompson AJ, Spears RJ, Zhu Y, Suits MDL, Williams SJ, Gilbert HJ, Davies GJ
OpenAccess logo Acta Crystallogr D Struct Biol 74 394-404 (2018)
Related entries: 6f8z, 6f91, 6f92

Cited: 6 times
EuropePMC logo PMID: 29717710

Abstract

A dominant human gut microbe, the well studied symbiont Bacteroides thetaiotaomicron (Bt), is a glyco-specialist that harbors a large repertoire of genes devoted to carbohydrate processing. Despite strong similarities among them, many of the encoded enzymes have evolved distinct substrate specificities, and through the clustering of cognate genes within operons termed polysaccharide-utilization loci (PULs) enable the fulfilment of complex biological roles. Structural analyses of two glycoside hydrolase family 92 α-mannosidases, BT3130 and BT3965, together with mechanistically relevant complexes at 1.8-2.5 Å resolution reveal conservation of the global enzyme fold and core catalytic apparatus despite different linkage specificities. Structure comparison shows that Bt differentiates the activity of these enzymes through evolution of a highly variable substrate-binding region immediately adjacent to the active site. These observations unveil a genetic/biochemical mechanism through which polysaccharide-processing bacteria can evolve new and specific biochemical activities from otherwise highly similar gene products.

Articles - 6f90 mentioned but not cited (1)

  1. Bacteroides thetaiotaomicron generates diverse α-mannosidase activities through subtle evolution of a distal substrate-binding motif. Thompson AJ, Spears RJ, Zhu Y, Suits MDL, Williams SJ, Gilbert HJ, Davies GJ. Acta Crystallogr D Struct Biol 74 394-404 (2018)


Articles citing this publication (5)

  1. Host glycan utilization within the Bacteroidetes Sus-like paradigm. Brown HA, Koropatkin NM. Glycobiology 31 697-706 (2021)
  2. Enterococcus faecalis α1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification. Li Y, Li R, Yu H, Sheng X, Wang J, Fisher AJ, Chen X. FEBS Lett 594 439-451 (2020)
  3. Plant N-glycan breakdown by human gut Bacteroides. Crouch LI, Urbanowicz PA, Baslé A, Cai ZP, Liu L, Voglmeir J, Melo Diaz JM, Benedict ST, Spencer DIR, Bolam DN. Proc Natl Acad Sci U S A 119 e2208168119 (2022)
  4. GH47 and Other Glycoside Hydrolases Catalyze Glycosidic Bond Cleavage with the Assistance of Substrate Super-arming at the Transition State. Quirke JCK, Crich D. ACS Catal 11 10308-10315 (2021)
  5. Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis. Kołaczkowski BM, Moroz OV, Blagova E, Davies GJ, Møller MS, Meyer AS, Westh P, Jensen K, Wilson KS, Krogh KBRM. Acta Crystallogr D Struct Biol 79 387-400 (2023)


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