1i5n
From Proteopedia
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| - | {{STRUCTURE_1i5n| PDB=1i5n | SCENE= }} | ||
| - | ===Crystal structure of the P1 domain of CheA from Salmonella typhimurium=== | ||
| - | {{ABSTRACT_PUBMED_11387324}} | ||
| - | == | + | ==Crystal structure of the P1 domain of CheA from Salmonella typhimurium== |
| - | [[1i5n]] is a 4 chain structure with sequence from [ | + | <StructureSection load='1i5n' size='340' side='right'caption='[[1i5n]], [[Resolution|resolution]] 2.14Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/1i5n_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: Salmonella enterica subsp. enterica serovar | + | <div class="pdbe-citations 1i5n" style="background-color:#fffaf0;"></div> |
| - | [[Category: Faurie | + | |
| - | [[Category: Guillet | + | ==See Also== |
| - | [[Category: Mourey | + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] |
| - | [[Category: Pedelacq | + | == References == |
| - | + | <references/> | |
| - | [[Category: Samama | + | __TOC__ |
| - | [[Category: Stock | + | </StructureSection> |
| - | [[Category: Tolstyk | + | [[Category: Large Structures]] |
| - | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | |
| - | + | [[Category: Da Re S]] | |
| + | [[Category: Faurie C]] | ||
| + | [[Category: Guillet V]] | ||
| + | [[Category: Mourey L]] | ||
| + | [[Category: Pedelacq J-D]] | ||
| + | [[Category: Samama J-P]] | ||
| + | [[Category: Stock JB]] | ||
| + | [[Category: Tolstyk T]] | ||
Current revision
Crystal structure of the P1 domain of CheA from Salmonella typhimurium
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