6FGX

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

Summary for 6FGX

• Entry DOI: 10.2210/pdb6fgx/pdb
• Related: 6FGJ
• Descriptor: GTP pyrophosphokinase, MAGNESIUM ION, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (4 entities in total)
• Functional Keywords: stringent response, alarmone, sas2, relp, transferase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 57247.30

Authors

Bange, G.,Vogt, M.,Steinchen, W.,Altegoer, F. (deposition date: 2018-01-11, release date: 2018-02-07, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)