6T96
Photorhabdus laumondii subsp. laumondii lectin PLL3
Summary for 6T96
| Entry DOI | 10.2210/pdb6t96/pdb |
| Descriptor | Lectin PLL3, SODIUM ION (3 entities in total) |
| Functional Keywords | lectin, beta-propeller, carbohydrate-binding protein, sugar binding protein |
| Biological source | Photorhabdus laumondii subsp. laumondii TTO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 40548.15 |
| Authors | Melicher, F.,Houser, J.,Fujdiarova, E.,Faltinek, L.,Wimmerova, M. (deposition date: 2019-10-26, release date: 2019-12-25, Last modification date: 2024-11-20) |
| Primary citation | Faltinek, L.,Fujdiarova, E.,Melicher, F.,Houser, J.,Kasakova, M.,Kondakov, N.,Kononov, L.,Parkan, K.,Vidal, S.,Wimmerova, M. Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed beta-Propeller Lectin Family. Molecules, 24:-, 2019 Cited by PubMed Abstract: The species is a Gram-negative bacteria of the family that is known for its mutualistic relationship with nematodes and pathogenicity toward insects. This study is focused on the characterization of the recombinant lectin PLL3 with an origin in subsp. . PLL3 belongs to the PLL family of lectins with a seven-bladed β-propeller fold. The binding properties of PLL3 were tested by hemagglutination assay, glycan array, isothermal titration calorimetry, and surface plasmon resonance, and its structure was determined by X-ray crystallography. Obtained data revealed that PLL3 binds similar carbohydrates to those that the other PLL family members bind, with some differences in the binding properties. PLL3 exhibited the highest affinity toward l-fucose and its derivatives but was also able to interact with -methylated glycans and other ligands. Unlike the other members of this family, PLL3 was discovered to be a monomer, which might correspond to a weaker avidity effect compared to homologous lectins. Based on the similarity to the related lectins and their proposed biological function, PLL3 might accompany them during the interaction of with both the nematode partner and the insect host. PubMed: 31835851DOI: 10.3390/molecules24244540 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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