期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-14754-7
关键词
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资金
- MINECO/FEDER EU [BFU2016-77427-C2-2-R, BFU2017-92223-EXP, SEV-2016-0644]
- Basque Government [KK-2019/00076]
- NIH [T32 AI095190, R01 GM096973]
- European Union [844905]
- Marie Curie Actions (MSCA) [844905] Funding Source: Marie Curie Actions (MSCA)
The human gut microbiota plays a central role not only in regulating the metabolism of nutrients but also promoting immune homeostasis, immune responses and protection against pathogen colonization. The genome of the Gram-negative symbiont Bacteroides thetaiotaomicron, a dominant member of the human intestinal microbiota, encodes polysaccharide utilization loci PULs, the apparatus required to orchestrate the degradation of a specific glycan. EndoBT-3987 is a key endo-beta-N-acetylglucosaminidase (ENGase) that initiates the degradation/processing of mammalian high-mannose-type (HM-type) N-glycans in the intestine. Here, we provide structural snapshots of EndoBT-3987, including the unliganded form, the EndoBT-3987-Man(9)GlcNAc(2)Asn substrate complex, and two EndoBT-3987-Man(9)GlcNAc and EndoBT-3987-Man(5)GlcNAc product complexes. In combination with alanine scanning mutagenesis and activity measurements we unveil the molecular mechanism of HM-type recognition and specificity for EndoBT-3987 and an important group of the GH18 ENGases, including EndoH, an enzyme extensively used in biotechnology, and for which the mechanism of substrate recognition was largely unknown.
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