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1ZHH

Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ

Summary for 1ZHH
Entry DOI10.2210/pdb1zhh/pdb
DescriptorAutoinducer 2-binding periplasmic protein luxP, Autoinducer 2 sensor kinase/phosphatase luxQ, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (4 entities in total)
Functional Keywordsperiplasmic binding protein, per/arnt/simple-minded (pas) fold, autoinducer-2 (ai-2), quorum sensing, sensor kinase, signaling protein
Biological sourceVibrio harveyi
More
Cellular locationPeriplasm (Probable): P54300
Cell inner membrane; Multi-pass membrane protein (Probable): P54302
Total number of polymer chains2
Total formula weight66909.97
Authors
Neiditch, M.B.,Federle, M.J.,Miller, S.T.,Bassler, B.L.,Hughson, F.M. (deposition date: 2005-04-25, release date: 2005-05-24, Last modification date: 2024-02-14)
Primary citationNeiditch, M.B.,Federle, M.J.,Miller, S.T.,Bassler, B.L.,Hughson, F.M.
Regulation of LuxPQ Receptor Activity by the Quorum-Sensing Signal Autoinducer-2.
Mol.Cell, 18:507-518, 2005
Cited by
PubMed Abstract: The extracellular signaling molecule autoinducer-2 (AI-2) mediates quorum-sensing communication in diverse bacterial species. In marine vibrios, binding of AI-2 to the periplasmic receptor LuxP modulates the activity of the inner membrane sensor kinase LuxQ, transducing the AI-2 information into the cytoplasm. Here, we show that Vibrio harveyi LuxP associates with LuxQ in both the presence and absence of AI-2. The 1.9 A X-ray crystal structure of apoLuxP, complexed with the periplasmic domain of LuxQ, reveals that the latter contains two tandem Per/ARNT/Simple-minded (PAS) folds. Thus, although many prokaryotic PAS folds themselves bind ligands, the LuxQ periplasmic PAS folds instead bind LuxP, monitoring its AI-2 occupancy. Mutations that disrupt the apoLuxP:LuxQ interface sensitize V. harveyi to AI-2, implying that AI-2 binding causes the replacement of one set of LuxP:LuxQ contacts with another. These conformational changes switch LuxQ between two opposing enzymatic activities, each of which conveys information to the cytoplasm about the cell density of the surrounding environment.
PubMed: 15916958
DOI: 10.1016/j.molcel.2005.04.020
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

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数据于2025-06-25公开中

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