3MHY

A New PII Protein Structure

3MHY の概要

• エントリーDOI: 10.2210/pdb3mhy/pdb
• 分子名称: PII-like protein Pz, 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE, ADENOSINE-5'-TRIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: pii protein, alpha-beta protein, homotrimer, signaling protein
• 由来する生物種: Azospirillum brasilense
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39912.61

構造登録者

Winkler, F.K.,Truan, D.,Li, X.D. (登録日: 2010-04-09, 公開日: 2010-06-09, 最終更新日: 2023-11-01)

主引用文献

Truan, D.,Huergo, L.F.,Chubatsu, L.S.,Merrick, M.,Li, X.D.,Winkler, F.K.
A new P(II) protein structure identifies the 2-oxoglutarate binding site.
J.Mol.Biol., 400:531-539, 2010

PubMed Abstract: P(II) proteins of bacteria, archaea, and plants regulate many facets of nitrogen metabolism. They do so by interacting with their target proteins, which can be enzymes, transcription factors, or membrane proteins. A key feature of the ability of P(II) proteins to sense cellular nitrogen status and to interact accordingly with their targets is their binding of the key metabolic intermediate 2-oxoglutarate (2-OG). However, the binding site of this ligand within P(II) proteins has been controversial. We have now solved the X-ray structure, at 1.4 A resolution, of the Azospirillum brasilense P(II) protein GlnZ complexed with MgATP and 2-OG. This structure is in excellent agreement with previous biochemical data on 2-OG binding to a variety of P(II) proteins and shows that 2-oxoglutarate binds within the cleft formed between neighboring subunits of the homotrimer. The 2-oxo acid moiety of bound 2-OG ligates the bound Mg(2+) together with three phosphate oxygens of ATP and the side chain of the T-loop residue Gln39. Our structure is in stark contrast to an earlier structure of the Methanococcus jannaschii GlnK1 protein in which the authors reported 2-OG binding to the T-loop of that P(II) protein. In the light of our new structure, three families of T-loop conformations, each associated with a distinct effector binding mode and characterized by a different interaction partner of the ammonium group of the conserved residue Lys58, emerge as a common structural basis for effector signal output by P(II) proteins.

PubMed: 20493877
DOI: 10.1016/j.jmb.2010.05.036

実験手法

X-RAY DIFFRACTION (1.4 Å)