1i5n

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[[Image:1i5n.gif|left|200px]]
 
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==Crystal structure of the P1 domain of CheA from Salmonella typhimurium==
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The line below this paragraph, containing "STRUCTURE_1i5n", creates the "Structure Box" on the page.
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<StructureSection load='1i5n' size='340' side='right'caption='[[1i5n]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1i5n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1i5n| PDB=1i5n | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5n OCA], [https://pdbe.org/1i5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5n RCSB], [https://www.ebi.ac.uk/pdbsum/1i5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHEA_SALTY CHEA_SALTY] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/1i5n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i5n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The x-ray crystal structure of the P1 or H domain of the Salmonella CheA protein has been solved at 2.1-A resolution. The structure is composed of an up-down up-down four-helix bundle that is typical of histidine phosphotransfer or HPt domains such as Escherichia coli ArcB(C) and Saccharomyces cerevisiae Ypd1. Loop regions and additional structural features distinguish all three proteins. The CheA domain has an additional C-terminal helix that lies over the surface formed by the C and D helices. The phosphoaccepting His-48 is located at a solvent-exposed position in the middle of the B helix where it is surrounded by several residues that are characteristic of other HPt domains. Mutagenesis studies indicate that conserved glutamate and lysine residues that are part of a hydrogen-bond network with His-48 are essential for the ATP-dependent phosphorylation reaction but not for the phosphotransfer reaction with CheY. These results suggest that the CheA-P1 domain may serve as a good model for understanding the general function of HPt domains in complex two-component phosphorelay systems.
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'''Crystal structure of the P1 domain of CheA from Salmonella typhimurium'''
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Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis.,Mourey L, Da Re S, Pedelacq JD, Tolstykh T, Faurie C, Guillet V, Stock JB, Samama JP J Biol Chem. 2001 Aug 17;276(33):31074-82. Epub 2001 May 31. PMID:11387324<ref>PMID:11387324</ref>
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==Overview==
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The x-ray crystal structure of the P1 or H domain of the Salmonella CheA protein has been solved at 2.1-A resolution. The structure is composed of an up-down up-down four-helix bundle that is typical of histidine phosphotransfer or HPt domains such as Escherichia coli ArcB(C) and Saccharomyces cerevisiae Ypd1. Loop regions and additional structural features distinguish all three proteins. The CheA domain has an additional C-terminal helix that lies over the surface formed by the C and D helices. The phosphoaccepting His-48 is located at a solvent-exposed position in the middle of the B helix where it is surrounded by several residues that are characteristic of other HPt domains. Mutagenesis studies indicate that conserved glutamate and lysine residues that are part of a hydrogen-bond network with His-48 are essential for the ATP-dependent phosphorylation reaction but not for the phosphotransfer reaction with CheY. These results suggest that the CheA-P1 domain may serve as a good model for understanding the general function of HPt domains in complex two-component phosphorelay systems.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1I5N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5N OCA].
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</div>
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<div class="pdbe-citations 1i5n" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis., Mourey L, Da Re S, Pedelacq JD, Tolstykh T, Faurie C, Guillet V, Stock JB, Samama JP, J Biol Chem. 2001 Aug 17;276(33):31074-82. Epub 2001 May 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11387324 11387324]
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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[[Category: Salmonella typhimurium]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Faurie, C.]]
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__TOC__
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[[Category: Guillet, V.]]
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</StructureSection>
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[[Category: Mourey, L.]]
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[[Category: Large Structures]]
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[[Category: Pedelacq, J D.]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Re, S Da.]]
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[[Category: Da Re S]]
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[[Category: Samama, J P.]]
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[[Category: Faurie C]]
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[[Category: Stock, J B.]]
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[[Category: Guillet V]]
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[[Category: Tolstyk, T.]]
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[[Category: Mourey L]]
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[[Category: Four-helix bundle]]
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[[Category: Pedelacq J-D]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:36:19 2008''
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[[Category: Samama J-P]]
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[[Category: Stock JB]]
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[[Category: Tolstyk T]]

Current revision

Crystal structure of the P1 domain of CheA from Salmonella typhimurium

PDB ID 1i5n

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