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-Structure paper
タイトル | A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 1860, Year 2024 |
掲載日 | 2024年2月29日 |
著者 | Xueliang Zhan / Kuo Zhang / Chenchen Wang / Qiao Fan / Xiujia Tang / Xi Zhang / Ke Wang / Yang Fu / Haihua Liang / |
PubMed 要旨 | Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a bacterial second messenger that modulates various processes including biofilm formation, motility, and host-microbe symbiosis. Numerous ...Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a bacterial second messenger that modulates various processes including biofilm formation, motility, and host-microbe symbiosis. Numerous studies have conducted comprehensive analysis of c-di-GMP. However, the mechanisms by which certain environmental signals such as iron control intracellular c-di-GMP levels are unclear. Here, we show that iron regulates c-di-GMP levels in Pseudomonas aeruginosa by modulating the interaction between an iron-sensing protein, IsmP, and a diguanylate cyclase, ImcA. Binding of iron to the CHASE4 domain of IsmP inhibits the IsmP-ImcA interaction, which leads to increased c-di-GMP synthesis by ImcA, thus promoting biofilm formation and reducing bacterial motility. Structural characterization of the apo-CHASE4 domain and its binding to iron allows us to pinpoint residues defining its specificity. In addition, the cryo-electron microscopy structure of ImcA in complex with a c-di-GMP analog (GMPCPP) suggests a unique conformation in which the compound binds to the catalytic pockets and to the membrane-proximal side located at the cytoplasm. Thus, our results indicate that a CHASE4 domain directly senses iron and modulates the crosstalk between c-di-GMP metabolic enzymes. |
リンク | Nat Commun / PubMed:38424057 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.9 - 3.2 Å |
構造データ | EMDB-37444, PDB-8wcn: PDB-8wct: |
化合物 | ChemComp-G2P: ChemComp-MG: ChemComp-GOL: ChemComp-HOH: |
由来 |
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キーワード | MEMBRANE PROTEIN / GGDEF domain / diguanylate cyclase activity / CHEASE4 domain / iron-sensetive |