2O66

Crystal Structure of Arabidopsis thaliana PII bound to citrate

2O66 の概要

• エントリーDOI: 10.2210/pdb2o66/pdb
• 関連するPDBエントリー: 2O67
• 分子名称: PII protein, CITRATE ANION (3 entities in total)
• 機能のキーワード: regulation of nitrogen and carbon metabolism, biosynthetic protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Plastid, chloroplast: Q9ZST4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44907.04

構造登録者

Mizuno, Y.,Berenger, B.,Moorhead, G.B.G.,Ng, K.K.S. (登録日: 2006-12-06, 公開日: 2007-02-20, 最終更新日: 2023-08-30)

主引用文献

Mizuno, Y.,Berenger, B.,Moorhead, G.B.,Ng, K.K.
Crystal Structure of Arabidopsis PII Reveals Novel Structural Elements Unique to Plants.
Biochemistry, 46:1477-1483, 2007

PubMed Abstract: The 1.9 A resolution crystal structure of PII from Arabidopsis thaliana reveals for the first time the molecular structure of a widely conserved regulator of carbon and nitrogen metabolism from a eukaryote. The structure provides a framework for understanding the arrangement of highly conserved residues shared with PII proteins from bacteria, archaea, and red algae as well as residues conserved only in plant PII. Most strikingly, a highly conserved segment at the N-terminus that is found only in plant PII forms numerous interactions with the alpha2 helix and projects from the surface of the homotrimer opposite to that occupied by the T-loop. In addition, solvent-exposed residues near the T-loop are highly conserved in plants but differ in prokaryotes. Several residues at the C-terminus that are also highly conserved only in plants contribute part of the ATP-binding site and likely participate in an ATP-induced conformational change. Structures of PII also reveal how citrate and malonate bind near the triphosphate binding site occupied by ATP in bacterial and archaeal PII proteins.

PubMed: 17279613
DOI: 10.1021/bi062149e

実験手法

X-RAY DIFFRACTION (1.9 Å)