1ZGR

Crystal structure of the Parkia platycephala seed lectin

Summary for 1ZGR

• Entry DOI: 10.2210/pdb1zgr/pdb
• Related: 1ZGS
• Descriptor: Mannose/glucose-specific lectin (2 entities in total)
• Functional Keywords: beta-prism, lectin, sugar binding protein
• Biological source: Parkia platycephala
• Total number of polymer chains: 2
• Total formula weight: 95133.65

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

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: 16185708
DOI: 10.1016/j.jmb.2005.08.055

Experimental method

X-RAY DIFFRACTION (2.5 Å)