3EBL

Crystal Structure of Rice GID1 complexed with GA4

3EBL の概要

• エントリーDOI: 10.2210/pdb3ebl/pdb
• 分子名称: Gibberellin receptor GID1, GIBBERELLIN A4, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total)
• 機能のキーワード: alpha/beta hydrolase, lipase, gibberellin signaling pathway, hydrolase, nucleus, receptor, hydrolase receptor
• 由来する生物種: Oryza sativa subsp. japonica (Rice)
• 細胞内の位置: Nucleus : Q6L545
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 249413.62

構造登録者

Shimada, A.,Nakatsu, T.,Ueguchi-Tanaka, M.,Kato, H.,Matsuoka, M. (登録日: 2008-08-28, 公開日: 2008-11-25, 最終更新日: 2024-03-20)

主引用文献

Shimada, A.,Ueguchi-Tanaka, M.,Nakatsu, T.,Nakajima, M.,Naoe, Y.,Ohmiya, H.,Kato, H.,Matsuoka, M.
Structural basis for gibberellin recognition by its receptor GID1.
Nature, 456:520-523, 2008

PubMed Abstract: Gibberellins (GAs) are phytohormones essential for many developmental processes in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4) and GA(3) at 1.9 A resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs except for an amino-terminal lid. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On the basis of the OsGID1 structure, we mutagenized important residues for GA binding and examined their binding activities. Almost all of them showed very little or no activity, confirming that the residues revealed by structural analysis are important for GA binding. The replacement of Ile 133 with Leu or Val-residues corresponding to those of the lycophyte Selaginella moellendorffii GID1s-caused an increase in the binding affinity for GA(34), a 2beta-hydroxylated GA(4). These observations indicate that GID1 originated from HSL and was further modified to have higher affinity and more strict selectivity for bioactive GAs by adapting the amino acids involved in GA binding in the course of plant evolution.

PubMed: 19037316
DOI: 10.1038/nature07546

実験手法

X-RAY DIFFRACTION (1.9 Å)