7fe1 | pdb_00007fe1

Crystal structure of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with methyl alpha-1,2-C-mannobioside

spinqualitylabelsall models 7fe1, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7fe1 is a 4 chain structure with sequence from Enterococcus faecalis ATCC 10100. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: 5II, ACY, CA, EDO, MAN, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q832K9_ENTFA Publication Abstract from PubMed The conformational changes in a sugar moiety along the hydrolytic pathway are key to understand the mechanism of glycoside hydrolases (GHs) and to design new inhibitors. The two predominant itineraries for mannosidases go via OS2 --> B2,5 --> 1S5 and 3S1 --> 3H4 --> 1C4. For the CAZy family 92, the conformational itinerary was unknown. Published complexes of Bacteroides thetaiotaomicron GH92 catalyst with a S-glycoside and mannoimidazole indicate a 4C1 --> 4H5/1S5 --> 1S5 mechanism. However, as observed with the GH125 family, S-glycosides may not act always as good mimics of GH's natural substrate. Here we present a cooperative study between computations and experiments where our results predict the E5 --> B2,5/1S5 --> 1S5 pathway for GH92 enzymes. Furthermore, we demonstrate the Michaelis complex mimicry of a new kind of C-disaccharides, whose biochemical applicability was still a chimera. Unlocking the hydrolytic mechanism of GH92 alpha-1,2-mannosidases: computation inspires using C-glycosides as Michaelis complex mimics.,Alonso-Gil S, Parkan K, Kaminsky J, Pohl R, Miyazaki T Chemistry. 2022 Jan 20. doi: 10.1002/chem.202200148. PMID:35049087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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