2014
Unraveling the Substrate Recognition Mechanism and Specificity of the Unusual Glycosyl Hydrolase Family 29 BT2192 from Bacteroides thetaiotaomicron
Abstract: Glycosyl hydrolase (GH) family 29 (CAZy database) consists of retaining α-l-fucosidases. We have identified BT2192, a protein from Bacteroides thetaiotaomicron, as the first GH29 representative exhibiting both weak α-l-fucosidase and β-d-galactosidase activities. Determination and analysis of X-ray structures of BT2192 in complex with β-d-galactoside competitive inhibitors showed a new binding mode different from that of known GH29 enzymes. Three point mutations, specific to BT2192, prevent the canonical GH29 …
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Cited by 22 publications
(18 citation statements)
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“…Of note, GH95 enzymes, also referred as 1,2-α-L-fucosidases (EC 3.2.1.63), specifically target α-1,2-fucosidic linkages 44,46 , thus corroborating our observation of FumA1 showing preference towards 2′-fucosyllactose. In contrast, FumA2 clusters with other previously characterized GH29 α-fucosidases, including BT_2970, BT_2192 and BT3798 from Bacteroides thetaiotaomicron VPI-5482 47–49 , Blon_2336 from Bifidobacterium longum subsp. infantis ATCC 15697 44 , TM0306 from Thermotoga maritima 50 and Afc2 from Clostridium perfrigens 46 .…”
Section: Resultsmentioning
confidence: 80%
“…Of note, GH95 enzymes, also referred as 1,2-α-L-fucosidases (EC 3.2.1.63), specifically target α-1,2-fucosidic linkages 44,46 , thus corroborating our observation of FumA1 showing preference towards 2′-fucosyllactose. In contrast, FumA2 clusters with other previously characterized GH29 α-fucosidases, including BT_2970, BT_2192 and BT3798 from Bacteroides thetaiotaomicron VPI-5482 47–49 , Blon_2336 from Bifidobacterium longum subsp. infantis ATCC 15697 44 , TM0306 from Thermotoga maritima 50 and Afc2 from Clostridium perfrigens 46 .…”
Section: Resultsmentioning
confidence: 80%
“…infantis and B. thetaiotaomicron, with C␣ r.m.s.d. values of 2.9, 2.9, and 3.5 Å of 299, 305, and 304 residues aligned, respectively (PDB codes 3MO4, 3EYP, and 3GZA) (19,61). 3 Both the overall folds of the N-terminal domains and active site residues are well conserved between FgFCO1 and bacterial homologues (Fig.…”
Section: Resultsmentioning
confidence: 98%
“…The catalytic N-terminal domain exhibits the familiar TIMbarrel fold reported for other GH29 enzymes (Guillotin et al, 2014;Lammerts van Bueren et al, 2010). However, -strands 5 and 6 are offset, with only one intra-main-chain hydrogen bond between them.…”
Section: Structure and Functionmentioning
confidence: 84%
