5xfh

Crystal structure of Orysata lectin in complex with biantennary N-glycan

spinqualitylabelsall models 5xfh, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xfh is a 2 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.903Å Ligands: BMA, GAL, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SALT_ORYSJ Publication Abstract from PubMed Mannose-binding type Jacalin-related lectins (mJRLs) bind to branched N-glycans via conserved sugar binding sites. Despite significant 3D structural similarities, each mJRL is known to have a unique binding preference towards various N-glycans. However, the molecular basis of varying binding preference is substantially unknown. Here we report a detailed comparison of N-glycan binding preference for two mJRLs, Orysata and Calsepa using frontal affinity chromatography (FAC), X-ray and molecular modeling. The FAC analysis using a panel of N-glycans shows difference in N-glycan binding preference between the lectins. Orysata shows broader specificity toward most high-mannose-type glycans as well as biantennary complex-type glycans bearing an extension on the Manalpha1-6 branch. Whereas, Calsepa shows narrow specificity to complex-type glycans with bisecting GlcNAc. The X-ray crystallographic structure reveals that two Orysata lectins bind to one biantennary N-glycan (2:1 binding) where one lectin binds to mannose of the alpha1-3 branch, while the other interacts with an N-acetylglucosamine of the alpha1-6 branch. In contrast, Calsepa shows 1:1 binding where alpha1-3 branch and core chitobiose region N-glycan interacts with lectin, while alpha1-6 branch is flipped back to the chitobiose core. Molecular dynamics study of Orysata bound to N-glycans substantiate possibility of two binding modes for each N-glycan. Binding free energies calculated separately for alpha1-3 and alpha1-6 branches of each N-glycan suggest both branches can bind to Orysata. Overall these results suggest that each branch of N-glycan has a distinct role in binding mJRLs and the non-binding branch can contribute significantly to the binding affinity and hence to the specificity. Distinct roles for each N-glycan branch interacting with mannose-binding type Jacalin-related lectins Orysata and Calsepa.,Nagae M, Mishra SK, Hanashima S, Tateno H, Yamaguchi Y Glycobiology. 2017 Sep 7. doi: 10.1093/glycob/cwx081. PMID:28973127 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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