2XZW

STRUCTURE OF PII FROM SYNECHOCOCCUS ELONGATUS IN COMPLEX WITH 2- OXOGLUTARATE AT LOW 2-OG CONCENTRATIONS

Replaces:  2XUN

Summary for 2XZW

• Entry DOI: 10.2210/pdb2xzw/pdb
• Related: 1QY7 2JJ4 2V5H 2XBP 2XG8 2XUL
• Descriptor: NITROGEN REGULATORY PROTEIN P-II, ADENOSINE-5'-TRIPHOSPHATE, 2-OXOGLUTARIC ACID, ... (5 entities in total)
• Functional Keywords: signaling protein
• Biological source: SYNECHOCOCCUS ELONGATUS
• Total number of polymer chains: 9
• Total formula weight: 120370.46

Authors

Zeth, K.,Chellamuthu, V.-R.,Forchhammer, K.,Fokina, O. (deposition date: 2010-11-29, release date: 2010-12-08, Last modification date: 2023-12-20)

Primary citation

Fokina, O.,Chellamuthu, V.-R.,Forchhammer, K.,Zeth, K.
Mechanism of 2-Oxoglutarate Signaling by the Synechococcus Elongatus Pii Signal Transduction Protein.
Proc.Natl.Acad.Sci.USA, 107:19760-, 2010

PubMed Abstract: P(II) proteins control key processes of nitrogen metabolism in bacteria, archaea, and plants in response to the central metabolites ATP, ADP, and 2-oxoglutarate (2-OG), signaling cellular energy and carbon and nitrogen abundance. This metabolic information is integrated by P(II) and transmitted to regulatory targets (key enzymes, transporters, and transcription factors), modulating their activity. In oxygenic phototrophs, the controlling enzyme of arginine synthesis, N-acetyl-glutamate kinase (NAGK), is a major P(II) target, whose activity responds to 2-OG via P(II). Here we show structures of the Synechococcus elongatus P(II) protein in complex with ATP, Mg(2+), and 2-OG, which clarify how 2-OG affects P(II)-NAGK interaction. P(II) trimers with all three sites fully occupied were obtained as well as structures with one or two 2-OG molecules per P(II) trimer. These structures identify the site of 2-OG located in the vicinity between the subunit clefts and the base of the T loop. The 2-OG is bound to a Mg(2+) ion, which is coordinated by three phosphates of ATP, and by ionic interactions with the highly conserved residues K58 and Q39 together with B- and T-loop backbone interactions. These interactions impose a unique T-loop conformation that affects the interactions with the P(II) target. Structures of P(II) trimers with one or two bound 2-OG molecules reveal the basis for anticooperative 2-OG binding and shed light on the intersubunit signaling mechanism by which P(II) senses effectors in a wide range of concentrations.

PubMed: 21041661
DOI: 10.1073/PNAS.1007653107

Experimental method

X-RAY DIFFRACTION (1.95 Å)