5DNU

Crystal structure of Striga KAI2-like protein in complex with karrikin

5DNU の概要

• エントリーDOI: 10.2210/pdb5dnu/pdb
• 関連するPDBエントリー: 5DNV 5DNW
• 分子名称: ShKAI2iB, 3-methyl-2H-furo[2,3-c]pyran-2-one, FORMIC ACID, ... (7 entities in total)
• 機能のキーワード: kai2 karrikin striga, hydrolase
• 由来する生物種: Striga hermonthica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31310.20

構造登録者

Xu, Y.,Miyakawa, T.,Nakamura, A.,Tanokura, M. (登録日: 2015-09-10, 公開日: 2016-08-17, 最終更新日: 2023-11-08)

主引用文献

Xu, Y.,Miyakawa, T.,Nakamura, H.,Nakamura, A.,Imamura, Y.,Asami, T.,Tanokura, M.
Structural basis of unique ligand specificity of KAI2-like protein from parasitic weed Striga hermonthica
Sci Rep, 6:31386-31386, 2016

PubMed Abstract: The perception of two plant germination inducers, karrikins and strigolactones, are mediated by the proteins KAI2 and D14. Recently, KAI2-type proteins from parasitic weeds, which are possibly related to seed germination induced by strigolactone, have been classified into three clades characterized by different responses to karrikin/strigolactone. Here we characterized a karrikin-binding protein in Striga (ShKAI2iB) that belongs to intermediate-evolving KAI2 and provided the structural bases for its karrikin-binding specificity. Binding assays showed that ShKAI2iB bound karrikins but not strigolactone, differing from other KAI2 and D14. The crystal structures of ShKAI2iB and ShKAI2iB-karrikin complex revealed obvious structural differences in a helix located at the entry of its ligand-binding cavity. This results in a smaller closed pocket, which is also the major cause of ShKAI2iB's specificity of binding karrikin. Our structural study also revealed that a few non-conserved amino acids led to the distinct ligand-binding profile of ShKAI2iB, suggesting that the evolution of KAI2 resulted in its diverse functions.

PubMed: 27507097
DOI: 10.1038/srep31386

実験手法

X-RAY DIFFRACTION (1.2 Å)