1jmw: Difference between revisions

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 <StructureSection load='1jmw' size='340' side='right'caption='[[1jmw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jmw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jmw]] is a 1 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=1JMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMW FirstGlance]. <br>
-</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=1jmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmw OCA], [https://pdbe.org/1jmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmw RCSB], [https://www.ebi.ac.uk/pdbsum/1jmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmw ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=1jmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmw OCA], [https://pdbe.org/1jmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmw RCSB], [https://www.ebi.ac.uk/pdbsum/1jmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MCP2_SALTY MCP2_SALTY]] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.  Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
+[https://www.uniprot.org/uniprot/MCP2_SALTY MCP2_SALTY] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.  Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1jmw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.
-Propagating conformational changes over long (and short) distances in proteins.,Yu EW, Koshland DE Jr Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9517-20. PMID:11504940<ref>PMID:11504940</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1jmw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Koshland, D E]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Yu, E W]]
+[[Category: Koshland Jr DE]]
-[[Category: Bacterial chemotactic receptor]]
+[[Category: Yu EW]]
-[[Category: Chemotaxis]]
-[[Category: Signaling protein]]