4OUE: Crystal Structure Of An A-l-fucosidase Gh29 From Bacteroides Thetaiotaomicron (bt2192) In Complex With Iptg

Citation:
Abstract
Glycosyl hydrolase (GH) family 29 (CAZy database) consists of retaining alpha-l-fucosidases. We have identified BT2192, a protein from Bacteroides thetaiotaomicron, as the first GH29 representative exhibiting both weak alpha-l-fucosidase and beta-d-galactosidase activities. Determination and analysis of X-ray structures of BT2192 in complex with beta-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 alpha-l-fucose from binding efficiently to the fucosidase-like active site relative to other GH29 enzymes. beta-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 A apart.
PDB ID: 4OUEDownload
MMDB ID: 117895
PDB Deposition Date: 2014/2/16
Updated in MMDB: 2014/04
Experimental Method:
x-ray diffraction
Resolution: 2.35  Å
Source Organism:
Similar Structures:
Biological Unit for 4OUE: monomeric; determined by author and by software (PISA)
Molecular Components in 4OUE
Label Count Molecule
Protein (1 molecule)
1
Putative Lipoprotein
Molecule annotation
Chemicals (3 molecules)
1
2
2
1
* Click molecule labels to explore molecular sequence information.

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