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6Q63

BT0459

Summary for 6Q63
Entry DOI10.2210/pdb6q63/pdb
DescriptorBeta-hexosaminidase, COPPER (II) ION, CALCIUM ION, ... (5 entities in total)
Functional Keywordsglycoside hydrolase family 20, complex n-glycans, microbiota, bacteroidetes, hydrolase
Biological sourceBacteroides thetaiotaomicron
Total number of polymer chains3
Total formula weight260719.04
Authors
Basle, A.,Crouch, L.,Bolam, D. (deposition date: 2018-12-10, release date: 2019-05-08, Last modification date: 2024-01-24)
Primary citationBriliute, J.,Urbanowicz, P.A.,Luis, A.S.,Basle, A.,Paterson, N.,Rebello, O.,Hendel, J.,Ndeh, D.A.,Lowe, E.C.,Martens, E.C.,Spencer, D.I.R.,Bolam, D.N.,Crouch, L.I.
Complex N-glycan breakdown by gut Bacteroides involves an extensive enzymatic apparatus encoded by multiple co-regulated genetic loci.
Nat Microbiol, 4:1571-1581, 2019
Cited by
PubMed Abstract: Glycans are the major carbon sources available to the human colonic microbiota. Numerous N-glycosylated proteins are found in the human gut, from both dietary and host sources, including immunoglobulins such as IgA that are secreted into the intestine at high levels. Here, we show that many mutualistic gut Bacteroides spp. have the capacity to utilize complex N-glycans (CNGs) as nutrients, including those from immunoglobulins. Detailed mechanistic studies using transcriptomic, biochemical, structural and genetic techniques reveal the pathway employed by Bacteroides thetaiotaomicron (Bt) for CNG degradation. The breakdown process involves an extensive enzymatic apparatus encoded by multiple non-adjacent loci and comprises 19 different carbohydrate-active enzymes from different families, including a CNG-specific endo-glycosidase activity. Furthermore, CNG degradation involves the activity of carbohydrate-active enzymes that have previously been implicated in the degradation of other classes of glycan. This complex and diverse apparatus provides Bt with the capacity to access the myriad different structural variants of CNGs likely to be found in the intestinal niche.
PubMed: 31160824
DOI: 10.1038/s41564-019-0466-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.44 Å)
Structure validation

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