6FGX

Crystal structure of the small alarmone synthethase 2 from Staphylococcus aureus bound to AMPCPP

6FGX の概要

• エントリーDOI: 10.2210/pdb6fgx/pdb
• 関連するPDBエントリー: 6FGJ
• 分子名称: GTP pyrophosphokinase, MAGNESIUM ION, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (4 entities in total)
• 機能のキーワード: stringent response, alarmone, sas2, relp, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57247.30

構造登録者

Bange, G.,Vogt, M.,Steinchen, W.,Altegoer, F. (登録日: 2018-01-11, 公開日: 2018-02-07, 最終更新日: 2024-01-17)

主引用文献

Steinchen, W.,Vogt, M.S.,Altegoer, F.,Giammarinaro, P.I.,Horvatek, P.,Wolz, C.,Bange, G.
Structural and mechanistic divergence of the small (p)ppGpp synthetases RelP and RelQ.
Sci Rep, 8:2195-2195, 2018

PubMed Abstract: The nutritional alarmones ppGpp and pppGpp (collectively: (p)ppGpp) are nucleotide-based second messengers enabling bacteria to respond to environmental and stress conditions. Several bacterial species contain two highly homologous (p)ppGpp synthetases named RelP (SAS2, YwaC) and RelQ (SAS1, YjbM). It is established that RelQ forms homotetramers that are subject to positive allosteric regulation by pppGpp, but structural and mechanistic insights into RelP lack behind. Here we present a structural and mechanistic characterization of RelP. In stark contrast to RelQ, RelP is not allosterically regulated by pppGpp and displays a different enzyme kinetic behavior. This discrepancy is evoked by different conformational properties of the guanosine-substrate binding site (G-Loop) of both proteins. Our study shows how minor structural divergences between close homologues result in new functional features during the course of molecular evolution.

PubMed: 29391580
DOI: 10.1038/s41598-018-20634-4

実験手法

X-RAY DIFFRACTION (2.9 Å)