2017
DOI: 10.1074/jbc.m117.777391
|View full text |Cite
|
Sign up to set email alerts
|

The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors

Abstract: The α--acetylgalactosaminidase from the probiotic bacterium (NagBb) belongs to the glycoside hydrolase family 129 and hydrolyzes the glycosidic bond of Tn-antigen (GalNAcα1-Ser/Thr). NagBb is involved in assimilation of-glycans on mucin glycoproteins by in the human gastrointestinal tract, but its catalytic mechanism has remained elusive because of a lack of sequence homology around putative catalytic residues and of other structural information. Here we report the X-ray crystal structure of NagBb, representin… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
16
0

Year Published

2018
2018
2024
2024

Publication Types

Select...
9

Relationship

2
7

Authors

Journals

citations
Cited by 22 publications
(17 citation statements)
references
References 58 publications
1
16
0
Order By: Relevance
“…In contrast, the B. dentium Bd1 or DSM 20436 genomes do not encode any GH33 enzymes, indicating the inability to remove sialic acid. Some bifidobacteria also code for GH101 and GH129, which includes a cell wall-anchored endo-α- N -acetylgalactosaminidase that can remove entire glycan structures from the mucin protein (81, 9498) (Fig. 2C and D).…”
Section: Resultsmentioning
confidence: 99%
“…In contrast, the B. dentium Bd1 or DSM 20436 genomes do not encode any GH33 enzymes, indicating the inability to remove sialic acid. Some bifidobacteria also code for GH101 and GH129, which includes a cell wall-anchored endo-α- N -acetylgalactosaminidase that can remove entire glycan structures from the mucin protein (81, 9498) (Fig. 2C and D).…”
Section: Resultsmentioning
confidence: 99%
“…GNB and LNB are known to be imported by the GNB/LNB transporter, an ATP-binding cassette-type (ABC) transporter [75,76]. GH129 α-N-acetylgalactosaminidase (NagBb) is able to act on α-N-acetylgalactosaminyl Ser (Tn antigen) to liberate GalNAc and Ser [26,77]. GalNAc-Ser/Thr can be generated from core 3 or core 4 mucin O-glycans after complete trimming by concerted actions of GHs and peptidases.…”
Section: Glycoside Hydrolases Involved In the Degradation Of Hmos/mucmentioning
confidence: 99%
“…This molecule is taken up by an as yet non-identified transporter and cleaved by the intracellular α- N -acetylgalactosaminidase NagBb that hydrolyzes the glycosidic bond between GalNAc and Ser/Thr amino acids ( Kiyohara et al, 2012 ). NagBb constitutes the first characterized member of the new GH129 family and the elucidation of its structure revealed the differences with GH101 enzymes regarding mechanism and substrate binding ( Sato et al, 2017 ).…”
Section: Conjugated Glycans: Glycoproteins and Glycolipidsmentioning
confidence: 99%