4d3g

Structure of PstA

spinqualitylabelsall models 4d3g, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d3g is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q2G229_STAA8] Publication Abstract from PubMed 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 a 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. While 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 reveal a series of conformational changes that result in the ordering of two anti-parallel beta-strands that protrude from each monomer and allowed us to propose a mechanism on how the PstA protein functions as a signaling transduction protein. 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.,Campeotto I, Zhang Y, Mladenov MG, Freemont PS, Grundling A J Biol Chem. 2014 Dec 11. pii: jbc.M114.621789. PMID:25505271 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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