4D3G
Structure of PstA
4D3G の概要
| エントリーDOI | 10.2210/pdb4d3g/pdb |
| 関連するPDBエントリー | 4D3H |
| 分子名称 | PSTA (1 entity in total) |
| 機能のキーワード | signaling protein, gram-positive, c-di-amp, psta |
| 由来する生物種 | STAPHYLOCOCCUS AUREUS |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13886.56 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 25505271DOI: 10.1074/JBC.M114.621789 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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