5OFZ
PllA lectin, apo
Summary for 5OFZ
| Entry DOI | 10.2210/pdb5ofz/pdb |
| Descriptor | Uncharacterized protein (2 entities in total) |
| Functional Keywords | plla, apo, lectin, sugar binding protein |
| Biological source | Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) |
| Total number of polymer chains | 4 |
| Total formula weight | 51878.18 |
| Authors | Koehnke, J.,Sikandar, A. (deposition date: 2017-07-11, release date: 2017-10-04, Last modification date: 2024-01-17) |
| Primary citation | Beshr, G.,Sikandar, A.,Jemiller, E.M.,Klymiuk, N.,Hauck, D.,Wagner, S.,Wolf, E.,Koehnke, J.,Titz, A. Photorhabdus luminescens lectin A (PllA): A new probe for detecting alpha-galactoside-terminating glycoconjugates. J. Biol. Chem., 292:19935-19951, 2017 Cited by PubMed Abstract: Lectins play important roles in infections by pathogenic bacteria, for example, in host colonization, persistence, and biofilm formation. The Gram-negative entomopathogenic bacterium symbiotically lives in insect-infecting nematodes and kills the insect host upon invasion by the nematode. The genome harbors the gene , 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 α-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° twist in subunit orientation leads to a peculiar quaternary structure compared with that of its ortholog LecA from We also investigated the utility of PllA as a probe for detecting α-galactosides. The α-Gal epitope is present on wild-type pig cells and is 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 summary, our biochemical and structural analyses of the lectin PllA have disclosed the structural basis for PllA's high specificity for α-galactoside-containing ligands, and we show that PllA can be used to visualize the α-Gal epitope on porcine tissues. PubMed: 28972138DOI: 10.1074/jbc.M117.812792 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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