1zhh | pdb_00001zhh
Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ
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Overview
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.
About this Structure
1ZHH is a Protein complex structure of sequences from Vibrio harveyi with NHE as ligand. Full crystallographic information is available from OCA.
Reference
Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2., Neiditch MB, Federle MJ, Miller ST, Bassler BL, Hughson FM, Mol Cell. 2005 May 27;18(5):507-18. PMID:15916958
Page seeded by OCA on Wed Nov 21 07:27:23 2007
