1ZGS
Parkia platycephala seed lectin in complex with 5-bromo-4-chloro-3-indolyl-a-D-mannose
Summary for 1ZGS
| Entry DOI | 10.2210/pdb1zgs/pdb |
| Related | 1ZGR |
| Descriptor | Mannose/glucose-specific lectin, 5-bromo-4-chloro-1H-indol-3-yl alpha-D-mannopyranoside (3 entities in total) |
| Functional Keywords | beta prism, lectin, x-man, sugar binding protein |
| Biological source | Parkia platycephala |
| Total number of polymer chains | 2 |
| Total formula weight | 97585.42 |
| Authors | Gallego del Sol, F.,Cavada, B.S.,Calvete, J.J. (deposition date: 2005-04-22, release date: 2005-10-11, Last modification date: 2024-03-13) |
| Primary citation | Gallego Del Sol, F.,Nagano, C.,Cavada, B.S.,Calvete, J.J. The first crystal structure of a mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain. J.Mol.Biol., 353:574-583, 2005 Cited by PubMed Abstract: The crystal structures of the apo and mannose-bound Parkia platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of beta-prism domains, and highlight the adaptability of the beta-prism fold as a building block in the evolution of plant lectins. The P.platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P.platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P.platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms. PubMed: 16185708DOI: 10.1016/j.jmb.2005.08.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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