3SNM

Crystal structure of a lectin from Canavalia maritima seeds complexed with Indole-3-Acetic Acid

3SNM の概要

• エントリーDOI: 10.2210/pdb3snm/pdb
• 分子名称: Concanavalin-A, CALCIUM ION, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: sugar binding protein, metal binding protein
• 由来する生物種: Canavalia lineata
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25881.54

構造登録者

Delatorre, P.,Silva-Filho, J.C.,Nobrega, R.B.,Rocha, B.C.,Cavada, B.S.,Gadelha, C.A.A.,Santi-Gadelha, T.,Alencar, K.L. (登録日: 2011-06-29, 公開日: 2012-08-01, 最終更新日: 2024-02-28)

主引用文献

Delatorre, P.,Silva-Filho, J.C.,Rocha, B.A.,Santi-Gadelha, T.,da Nobrega, R.B.,Gadelha, C.A.,do Nascimento, K.S.,Nagano, C.S.,Sampaio, A.H.,Cavada, B.S.
Interactions between indole-3-acetic acid (IAA) with a lectin from Canavalia maritima seeds reveal a new function for lectins in plant physiology.
Biochimie, 95:1697-1703, 2013

PubMed Abstract: Indole-3-acetic acid (IAA) bound is considered a storage molecule and is inactive. However, some studies have proposed an additional possible regulatory mechanism based on the ability of lectins to form complexes with IAA. We report the first crystal structure of ConM in complex with IAA at 2.15 Å resolution. Based on a tetrameric model of the complex, we hypothesize how the lectin controls the availability of IAA during the early seedling stages, indicating a possible new physiological role for these proteins. A free indole group is also bound to the protein. The ConM interaction with different forms of IAA is a strategy to render the phytohormone unavailable to the cell. Thus, this new physiological role proposed for legume lectins might be a novel mechanism by which IAA levels are decreased in addition to the destruction and formation of new complexes in the later stages of seed germination.

PubMed: 23727478
DOI: 10.1016/j.biochi.2013.05.008

実験手法

X-RAY DIFFRACTION (2.15 Å)