5YA1
crystal structure of LsrK-HPr complex with ATP
5YA1 の概要
エントリーDOI | 10.2210/pdb5ya1/pdb |
分子名称 | Autoinducer-2 kinase, Phosphocarrier protein HPr, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
機能のキーワード | atp binding, structural protein |
由来する生物種 | Escherichia coli (strain K12) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 138215.15 |
構造登録者 | |
主引用文献 | Ha, J.H.,Hauk, P.,Cho, K.,Eo, Y.,Ma, X.,Stephens, K.,Cha, S.,Jeong, M.,Suh, J.Y.,Sintim, H.O.,Bentley, W.E.,Ryu, K.S. Evidence of link between quorum sensing and sugar metabolism inEscherichia colirevealed via cocrystal structures of LsrK and HPr Sci Adv, 4:eaar7063-eaar7063, 2018 Cited by PubMed Abstract: Quorum sensing (QS), a bacterial process that regulates population-scale behavior, is mediated by small signaling molecules, called autoinducers (AIs), that are secreted and perceived, modulating a "collective" phenotype. Because the autoinducer AI-2 is secreted by a wide variety of bacterial species, its "perception" cues bacterial behavior. This response is mediated by the (LuxS-regulated) operon that includes the AI-2 transporter LsrACDB and the kinase LsrK. We report that HPr, a phosphocarrier protein central to the sugar phosphotransferase system of , copurifies with LsrK. Cocrystal structures of an LsrK/HPr complex were determined, and the effects of HPr and phosphorylated HPr on LsrK activity were assessed. LsrK activity is inhibited when bound to HPr, revealing new linkages between QS activity and sugar metabolism. These findings help shed new light on the abilities of bacteria to rapidly respond to changing nutrient levels at the population scale. They also suggest new means of manipulating QS activity among bacteria and within various niches. PubMed: 29868643DOI: 10.1126/sciadv.aar7063 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.701 Å) |
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