1zhh

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[[Image:1zhh.gif|left|200px]]
[[Image:1zhh.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1zhh", creates the "Structure Box" on the page.
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|GENE= luxP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 Vibrio harveyi]), luxQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 Vibrio harveyi])
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{{STRUCTURE_1zhh| PDB=1zhh | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zhh OCA], [http://www.ebi.ac.uk/pdbsum/1zhh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zhh RCSB]</span>
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'''Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ'''
'''Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ'''
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[[Category: Miller, S T.]]
[[Category: Miller, S T.]]
[[Category: Neiditch, M B.]]
[[Category: Neiditch, M B.]]
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[[Category: autoinducer-2 (ai-2)]]
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[[Category: Periplasmic binding protein]]
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[[Category: per/arnt/simple-minded (pas) fold]]
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[[Category: Quorum sensing]]
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[[Category: periplasmic binding protein]]
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[[Category: Sensor kinase]]
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[[Category: quorum sensing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:37:42 2008''
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[[Category: sensor kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:36:46 2008''
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Revision as of 14:37, 3 May 2008

Image:1zhh.gif

Template:STRUCTURE 1zhh

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


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. 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 Sat May 3 17:37:42 2008

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