2hje
From Proteopedia
(New page: 200px<br /><applet load="2hje" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hje, resolution 1.70Å" /> '''Crystal structure of...) |
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| - | [[Image:2hje.gif|left|200px]]<br /><applet load="2hje" size=" | + | [[Image:2hje.gif|left|200px]]<br /><applet load="2hje" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hje, resolution 1.70Å" /> | caption="2hje, resolution 1.70Å" /> | ||
'''Crystal structure of Vibrio harveyi LuxQ periplasmic domain'''<br /> | '''Crystal structure of Vibrio harveyi LuxQ periplasmic domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacteria sense their environment using receptors of the histidine sensor | + | Bacteria sense their environment using receptors of the histidine sensor kinase family, but how kinase activity is regulated by ligand binding is not well understood. Autoinducer-2 (AI-2), a secreted signaling molecule originally identified in studies of the marine bacterium Vibrio harveyi, regulates quorum-sensing responses and allows communication between different bacterial species. AI-2 signal transduction in V. harveyi requires the integral membrane receptor LuxPQ, comprised of periplasmic binding protein (LuxP) and histidine sensor kinase (LuxQ) subunits. Combined X-ray crystallographic and functional studies show that AI-2 binding causes a major conformational change within LuxP, which in turn stabilizes a quaternary arrangement in which two LuxPQ monomers are asymmetrically associated. We propose that formation of this asymmetric quaternary structure is responsible for repressing the kinase activity of both LuxQ subunits and triggering the transition of V. harveyi into quorum-sensing mode. |
==About this Structure== | ==About this Structure== | ||
| - | 2HJE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with NI as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] Full crystallographic information is available from [http:// | + | 2HJE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
| - | [[Category: Hughson, F | + | [[Category: Hughson, F M.]] |
| - | [[Category: Kelly, R | + | [[Category: Kelly, R C.]] |
| - | [[Category: Neiditch, M | + | [[Category: Neiditch, M B.]] |
[[Category: NI]] | [[Category: NI]] | ||
[[Category: autoinducer-2 (ai-2)]] | [[Category: autoinducer-2 (ai-2)]] | ||
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[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:30 2008'' |
Revision as of 15:42, 21 February 2008
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Crystal structure of Vibrio harveyi LuxQ periplasmic domain
Overview
Bacteria sense their environment using receptors of the histidine sensor kinase family, but how kinase activity is regulated by ligand binding is not well understood. Autoinducer-2 (AI-2), a secreted signaling molecule originally identified in studies of the marine bacterium Vibrio harveyi, regulates quorum-sensing responses and allows communication between different bacterial species. AI-2 signal transduction in V. harveyi requires the integral membrane receptor LuxPQ, comprised of periplasmic binding protein (LuxP) and histidine sensor kinase (LuxQ) subunits. Combined X-ray crystallographic and functional studies show that AI-2 binding causes a major conformational change within LuxP, which in turn stabilizes a quaternary arrangement in which two LuxPQ monomers are asymmetrically associated. We propose that formation of this asymmetric quaternary structure is responsible for repressing the kinase activity of both LuxQ subunits and triggering the transition of V. harveyi into quorum-sensing mode.
About this Structure
2HJE is a Single protein structure of sequence from Vibrio harveyi with as ligand. Active as Histidine kinase, with EC number 2.7.13.3 Full crystallographic information is available from OCA.
Reference
Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing., Neiditch MB, Federle MJ, Pompeani AJ, Kelly RC, Swem DL, Jeffrey PD, Bassler BL, Hughson FM, Cell. 2006 Sep 22;126(6):1095-108. PMID:16990134
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