4CNY

Structure of PII signaling protein GlnZ from Azospirillum brasilense

4CNY の概要

• エントリーDOI: 10.2210/pdb4cny/pdb
• 関連するPDBエントリー: 3MHY 4CNZ 4CO0 4CO1 4CO2 4CO3 4CO4 4CO5
• 分子名称: PII-LIKE PROTEIN PZ, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: signaling protein, glnk-like
• 由来する生物種: AZOSPIRILLUM BRASILENSE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12572.02

構造登録者

Truan, D.,Li, X.-D.,Winkler, F.K. (登録日: 2014-01-25, 公開日: 2014-05-28, 最終更新日: 2023-12-20)

主引用文献

Truan, D.,Bjelic, S.,Li, X.,Winkler, F.K.
Structure and Thermodynamics of Effector Molecule Binding to the Nitrogen Signal Transduction Pii Protein Glnz from Azospirillum Brasilense.
J.Mol.Biol., 426:2783-, 2014

PubMed Abstract: The trimeric PII signal transduction proteins regulate the function of a variety of target proteins predominantly involved in nitrogen metabolism. ATP, ADP and 2-oxoglutarate (2-OG) are key effector molecules influencing PII binding to targets. Studies of PII proteins have established that the 20-residue T-loop plays a central role in effector sensing and target binding. However, the specific effects of effector binding on T-loop conformation have remained poorly documented. We present eight crystal structures of the Azospirillum brasilense PII protein GlnZ, six of which are cocrystallized and liganded with ADP or ATP. We find that interaction with the diphosphate moiety of bound ADP constrains the N-terminal part of the T-loop in a characteristic way that is maintained in ADP-promoted complexes with target proteins. In contrast, the interactions with the triphosphate moiety in ATP complexes are much more variable and no single predominant interaction mode is apparent except for the ternary MgATP/2-OG complex. These conclusions can be extended to most investigated PII proteins of the GlnB/GlnK subfamily. Unlike reported for other PII proteins, microcalorimetry reveals no cooperativity between the three binding sites of GlnZ trimers for any of the three effectors under carefully controlled experimental conditions.

PubMed: 24846646
DOI: 10.1016/J.JMB.2014.05.008

実験手法

X-RAY DIFFRACTION (1.2 Å)