4OUE
Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG
Summary for 4OUE
| Entry DOI | 10.2210/pdb4oue/pdb |
| Related | 4OZO |
| Descriptor | Putative lipoprotein, GLYCEROL, 1-methylethyl 1-thio-beta-D-galactopyranoside, ... (4 entities in total) |
| Functional Keywords | beta sandwich, glycosyl hydrolase gh29, hydrolase |
| Biological source | Bacteroides thetaiotaomicron |
| Total number of polymer chains | 2 |
| Total formula weight | 107681.32 |
| Authors | Lafite, P.,Daniellou, R.,Guillotin, L. (deposition date: 2014-02-16, release date: 2014-02-26, Last modification date: 2024-02-28) |
| Primary citation | Guillotin, L.,Lafite, P.,Daniellou, R. Unraveling the Substrate Recognition Mechanism and Specificity of the Unusual Glycosyl Hydrolase Family 29 BT2192 from Bacteroides thetaiotaomicron. Biochemistry, 53:1447-1455, 2014 Cited by PubMed 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 substrate α-l-fucose from binding efficiently to the fucosidase-like active site relative to other GH29 enzymes. β-d-Galactoside analogues bind and interact in a second pocket, which is not visible in other reported GH29 structures. Molecular simulations helped in the assessment of the flexibility of both substrates in their respective pocket. Hydrolysis of the fucosyl moiety from the putative natural substrates like 3-fucosyllactose or Lewis(X) antigen would be mainly due to the efficient interactions with the galactosyl moiety, in the second binding site, located more than 6-7 Å apart. PubMed: 24527659DOI: 10.1021/bi400951q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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