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5YA2

Crystal structure of LsrK-HPr complex with ADP

Summary for 5YA2
Entry DOI10.2210/pdb5ya2/pdb
DescriptorAutoinducer-2 kinase, Phosphocarrier protein HPr, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
Functional Keywordsquorum sensing, lsrk, hpr, complex, adp binding, structural protein
Biological sourceEscherichia coli (strain K12)
More
Total number of polymer chains4
Total formula weight137628.90
Authors
Ryu, K.S.,Ha, J.H. (deposition date: 2017-08-30, release date: 2018-07-11, Last modification date: 2024-03-27)
Primary citationHa, 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: 29868643
DOI: 10.1126/sciadv.aar7063
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.701 Å)
Structure validation

226707

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