5YA0
Crystal structure of LsrK and HPr complex
Summary for 5YA0
| Entry DOI | 10.2210/pdb5ya0/pdb |
| Descriptor | Autoinducer-2 kinase, Phosphocarrier protein HPr, HEXANE-1,6-DIOL, ... (5 entities in total) |
| Functional Keywords | quorum sensing, structural protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 4 |
| Total formula weight | 136774.50 |
| Authors | |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.997 Å) |
Structure validation
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