5mul | pdb_00005mul

Glycoside Hydrolase BT3686 bound to Glucuronic Acid

spinqualitylabelsall models 5mul, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mul is a 1 chain structure with sequence from Bacteroides thetaiotaomicron VPI-5482. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.39Å Ligands: BDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8A1H5_BACTN Publication Abstract from PubMed The human gut microbiota use complex carbohydrates as major nutrients. The requirement for an efficient glycan degrading systems exerts a major selection pressure on this microbial community. Thus, we propose that these bacteria represent a substantial resource for discovering novel carbohydrate active enzymes. To test this hypothesis, we focused on enzymes that hydrolyze rhamnosidic bonds, as cleavage of these linkages is chemically challenging and there is a paucity of information on l-rhamnosidases. Here we screened the activity of enzymes derived from the human gut microbiota bacterium Bacteroides thetaiotaomicron, which are up-regulated in response to rhamnose-containing glycans. We identified an alpha-l-rhamnosidase, BT3686, which is the founding member of a glycoside hydrolase (GH) family, GH145. In contrast to other rhamnosidases, BT3686 cleaved l-Rha-alpha1,4-d-GlcA linkages through a retaining double-displacement mechanism. The crystal structure of BT3686 showed that the enzyme displayed a type A seven-bladed beta-propeller fold. Mutagenesis and crystallographic studies, including the structure of BT3686 in complex with the reaction product GlcA, revealed a location for the active site among beta-propeller enzymes cited on the posterior surface of the rhamnosidase. In contrast to the vast majority of GH, the catalytic apparatus of BT3686 does not comprise a pair of carboxylic acid residues but, uniquely, a single histidine functions as the only discernable catalytic amino acid. Intriguingly, the histidine, His48, is not invariant in GH145; however, when engineered into structural homologs lacking the imidazole residue, alpha-l-rhamnosidase activity was established. The potential contribution of His48 to the catalytic activity of BT3686 is discussed. Unusual active site location and catalytic apparatus in a glycoside hydrolase family.,Munoz-Munoz J, Cartmell A, Terrapon N, Henrissat B, Gilbert HJ Proc Natl Acad Sci U S A. 2017 Apr 10. pii: 201701130. doi:, 10.1073/pnas.1701130114. PMID:28396425 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neuraminidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA