6li7

Crystal Structure of Lectin from Pleurotus ostreatus in complex with GalNAc

spinqualitylabelsall models 6li7, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.098Å Ligands: CA, GOL, NAG, NGA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Carbohydrate recognition is established as a property of lectins and implicated in many functions including immunity and defense against pathogens. Many lectins are characterized and proposed for various applications owing to the above said recognition. The crystal structure of a lectin from Pleurotus ostreatus has been determined and shown to be calcium dependent. The overall structure is a tandem repeat of two beta-jelly roll domains, a new fold for lectins. The calcium dependence of sugar binding is analyzed in-detail through isothermal titration calorimetry. The serendipitous observation of malonate and glycerol, the intentional N-Acetyl-D-galactosamine, D-Galactose and L-Rhamnose binding to Pleurotus ostreatus lectin by Ca(2+) coordination revealed that the binding site is promiscuous. Among these sugars, Rhamnose binding found to be thermodynamically most favourable. In all these structures, a vicinal diol motif, one at axial and the other at equatorial positions could be established as a specific requirement for binding. Interestingly, when compared with other calcium mediated lectin structures; this geometric requirement is found conserved. This observation could lead to the conclusion that lectins are not 'molecule specific' but 'geometry specific' so that any molecule not necessarily a sugar may be recognized by this lectin if the geometry exists. Crystallographic and calorimetric analysis on Pleurotus ostreatus lectin and its sugar complexes - promiscuous binding driven by geometry.,Vajravijayan S, Pletnev S, Luo Z, Pletnev VZ, Nandhagopal N, Gunasekaran K Int J Biol Macromol. 2020 Jun 1;152:862-872. doi: 10.1016/j.ijbiomac.2020.02.294., Epub 2020 Feb 26. PMID:32112837 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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