4D3H

Structure of PstA

Summary for 4D3H

• Entry DOI: 10.2210/pdb4d3h/pdb
• Related: 4D3G
• Descriptor: PSTA, (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide (3 entities in total)
• Functional Keywords: signalling protein, gram-positive, c-di-amp
• Biological source: STAPHYLOCOCCUS AUREUS
• Total number of polymer chains: 3
• Total formula weight: 43634.91

Authors

Campeotto, I.,Freemont, P.,Grundling, A. (deposition date: 2014-10-22, release date: 2014-12-24, Last modification date: 2023-12-20)

Primary citation

Campeotto, I.,Zhang, Y.,Mladenov, M.G.,Freemont, P.S.,Grundling, A.
Complex Structure and Biochemical Characterization of the Staphylococcus Aureus Cyclic Di-AMP Binding Protein Psta, the Founding Member of a New Signal Transduction Protein Family
J.Biol.Chem., 290:2888-, 2015

PubMed Abstract: Signaling nucleotides are integral parts of signal transduction systems allowing bacteria to cope with and rapidly respond to changes in the environment. The Staphylococcus aureus PII-like signal transduction protein PstA was recently identified as a cyclic diadenylate monophosphate (c-di-AMP)-binding protein. Here, we present the crystal structures of the apo- and c-di-AMP-bound PstA protein, which is trimeric in solution as well as in the crystals. The structures combined with detailed bioinformatics analysis revealed that the protein belongs to a new family of proteins with a similar core fold but with distinct features to classical PII proteins, which usually function in nitrogen metabolism pathways in bacteria. The complex structure revealed three identical c-di-AMP-binding sites per trimer with each binding site at a monomer-monomer interface. Although distinctly different from other cyclic-di-nucleotide-binding sites, as the half-binding sites are not symmetrical, the complex structure also highlighted common features for c-di-AMP-binding sites. A comparison between the apo and complex structures revealed a series of conformational changes that result in the ordering of two anti-parallel β-strands that protrude from each monomer and allowed us to propose a mechanism on how the PstA protein functions as a signaling transduction protein.

PubMed: 25505271
DOI: 10.1074/JBC.M114.621789

Experimental method

X-RAY DIFFRACTION (2 Å)