5ofi

PllA lectin, Fluorophore carbohydrate complex

spinqualitylabelsall models 5ofi, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ofi is a 8 chain structure with sequence from Photorhabdus luminescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 9TQ, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLLA_PHOLL Lectin that specifically binds alpha-galactoside-terminating glycoconjugates. Shows high apparent binding to the alpha-Gal epitope (Gal-alpha-1,3-Gal-beta-1,4-GlcNAc terminating glycans) as well as to Gal-alpha-1,4-GlcNAc and Gal-alpha-1,3-GalNAc. Gal-alpha-1,3-GalNAc may be one natural ligand bound by PllA both in the nematode symbiont and in infected insects. Publication Abstract from PubMed Lectins play important roles in infections by pathogenic bacteria, for example, in host colonization, persistence and biofilm formation. The Gram-negative entomopathogenic bacterium Photorhabdus luminescens symbiotically lives in insect-infecting Heterorhabditis nematodes and kills the insect host upon invasion by the nematode. The P. luminescens genome harbors the gene plu2096 coding for a novel lectin that we named PllA. We analyzed the binding properties of purified PllA with a glycan array and a binding assay in solution. Both assays revealed a strict specificity of PllA for alpha-galactoside-terminating glycoconjugates. The crystal structures of apo PllA and complexes with three different ligands revealed the molecular basis for the strict specificity of this lectin. Furthermore, we found that a 90 degree twist in subunit orientation leads to a peculiar quaternary structure compared with that of its ortholog LecA from Pseudomonas aeruginosa. We also investigated the utility of PllA as a probe for detecting alpha-galactosides. The alpha-Gal epitope is present on wild-type pig cells and the main reason for hyperacute organ rejection in pig to primate xenotransplantation. We noted that PllA specifically recognizes this epitope on the glycan array and demonstrated that PllA can be used as a fluorescent probe to detect this epitope on primary porcine cells in vitro. In summary, our biochemical and structural analyses of the P. luminescens lectin PllA have disclosed the structural basis for PllAs high specificity for alpha-galactoside-containing ligands, and we show that PllA can be used to visualize alpha-Gal epitope on porcine tissues. Photorhabdus luminescens lectin A (PllA) - a new probe for detecting alpha-galactoside-terminating glycoconjugates.,Beshr G, Sikandar A, Jemiller EM, Klymiuk N, Hauck D, Wagner S, Wolf E, Koehnke J, Titz A J Biol Chem. 2017 Sep 28. pii: jbc.M117.812792. doi: 10.1074/jbc.M117.812792. PMID:28972138 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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