1zhh
From Proteopedia
(New page: 200px<br /><applet load="1zhh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zhh, resolution 1.94Å" /> '''Crystal Structure of...) |
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| - | [[Image:1zhh.gif|left|200px]]<br /><applet load="1zhh" size=" | + | [[Image:1zhh.gif|left|200px]]<br /><applet load="1zhh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zhh, resolution 1.94Å" /> | caption="1zhh, resolution 1.94Å" /> | ||
'''Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ'''<br /> | '''Crystal Structure of the Apo Form of Vibrio Harveyi LUXP Complexed with the Periplasmic Domain of LUXQ'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The extracellular signaling molecule autoinducer-2 (AI-2) mediates | + | 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== | ==About this Structure== | ||
| - | 1ZHH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with NHE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZHH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with <scene name='pdbligand=NHE:'>NHE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
| - | [[Category: Bassler, B | + | [[Category: Bassler, B L.]] |
| - | [[Category: Federle, M | + | [[Category: Federle, M J.]] |
| - | [[Category: Hughson, F | + | [[Category: Hughson, F M.]] |
| - | [[Category: Miller, S | + | [[Category: Miller, S T.]] |
| - | [[Category: Neiditch, M | + | [[Category: Neiditch, M B.]] |
[[Category: NHE]] | [[Category: NHE]] | ||
[[Category: autoinducer-2 (ai-2)]] | [[Category: autoinducer-2 (ai-2)]] | ||
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[[Category: sensor kinase]] | [[Category: sensor kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:33 2008'' |
Revision as of 14:15, 21 February 2008
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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 with 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
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