1LR5

Crystal structure of auxin binding protein

1LR5 の概要

• エントリーDOI: 10.2210/pdb1lr5/pdb
• 関連するPDBエントリー: 1LRH
• 分子名称: Auxin binding protein 1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (4 entities in total)
• 機能のキーワード: beta jellyroll, double stranded beta helix, germin-like protein, protein binding
• 由来する生物種: Zea mays
• 細胞内の位置: Endoplasmic reticulum lumen: P13689
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78200.73

構造登録者

Woo, E.J.,Marshall, J.,Bauley, J.,Chen, J.-G.,Venis, M.,Napier, R.M.,Pickersgill, R.W. (登録日: 2002-05-14, 公開日: 2002-06-19, 最終更新日: 2024-11-20)

主引用文献

Woo, E.J.,Marshall, J.,Bauly, J.,Chen, J.G.,Venis, M.,Napier, R.M.,Pickersgill, R.W.
Crystal structure of auxin-binding protein 1 in complex with auxin.
EMBO J., 21:2877-2885, 2002

PubMed Abstract: The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.

PubMed: 12065401
DOI: 10.1093/emboj/cdf291

実験手法

X-RAY DIFFRACTION (1.9 Å)