1ZGR

Crystal structure of the Parkia platycephala seed lectin

1ZGR の概要

• エントリーDOI: 10.2210/pdb1zgr/pdb
• 関連するPDBエントリー: 1ZGS
• 分子名称: Mannose/glucose-specific lectin (2 entities in total)
• 機能のキーワード: beta-prism, lectin, sugar binding protein
• 由来する生物種: Parkia platycephala
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95133.65

構造登録者

Gallego del Sol, F.,Cavada, B.S.,Calvete, J.J. (登録日: 2005-04-22, 公開日: 2005-10-11, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)