3wqw | pdb_00003wqw

Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6

spinqualitylabelsall models 3wqw, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wqw is a 1 chain structure with sequence from Ostrinia furnacalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: EPE, GCS, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2V6H4_OSTFU Publication Abstract from PubMed Small-molecule inhibitors against chitinases have potential applications as pesticides, fungicides, and antiasthmatics. Here, we report a series of fully deacetylated chitooligosaccharides (GlcN)2-7 can act as inhibitors against the insect chitinase OfChtI, the human chitinase HsCht, and the bacterial chitinases SmChiA and SmChiB with IC50 values at muM to mM levels. The injection of mixed (GlcN)2-7 into the 5th instar larvae of the insect Ostrinia furnacalis resulted in 85% of the larvae being arrested at the larval stage and death after 10 days, also suggesting (GlcN)2-7 might inhibit OfChtI in vivo. Crystal structures of the catalytic domain of OfChtI (OfChtI-CAD) complexed with (GlcN)5, 6 were obtained at resolutions of 2.0 A. These structures, together with mutagenesis and thermodynamic analysis, suggested that the inhibition was strongly related to the interaction between the -1 GlcN residue of the inhibitor and the catalytic E148 of the enzyme. Structure-based comparison showed that the fully deacetylated chitooligosaccharides mimic the substrate chitooligosaccharides by binding in the active cleft. This work first reports the inhibitory activity and proposed inhibitory mechanism of fully deacetylated chitooligosaccharides. Because the fully deacetylated chitooligosaccharides can be easily derived from chitin, one of the most abundant nature materials, this work also provides a platform for developing eco-friendly inhibitors against chitinases. Fully deacetylated chitooligosaccharides act as efficient glycoside hydrolase family18 chitinase inhibitors.,Chen L, Zhou Y, Qu M, Zhao Y, Yang Q J Biol Chem. 2014 May 14. pii: jbc.M114.564534. PMID:24828498 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase 3D structures

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