1a2o: Difference between revisions

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-{{Seed}}
-[[Image:1a2o.png|left|200px]]
-<!--
+==STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN==
-The line below this paragraph, containing "STRUCTURE_1a2o", creates the "Structure Box" on the page.
+<StructureSection load='1a2o' size='340' side='right'caption='[[1a2o]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1a2o]] is a 2 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=1A2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2O FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=1a2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2o OCA], [https://pdbe.org/1a2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2o RCSB], [https://www.ebi.ac.uk/pdbsum/1a2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2o ProSAT]</span></td></tr>
-{{STRUCTURE_1a2o|  PDB=1a2o  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHEB_SALTY CHEB_SALTY] Responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The MCP methylation state of the cell is crucial for sensory responses and adaptations.[HAMAP-Rule:MF_00099]
+== 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/a2/1a2o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1a2o ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We report the x-ray crystal structure of the methylesterase CheB, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Methylesterase CheB and methyltransferase CheR modulate signaling output of the chemotaxis receptors by controlling the level of receptor methylation. The structure of CheB, which consists of an N-terminal regulatory domain and a C-terminal catalytic domain joined by a linker, was solved by molecular replacement methods using independent search models for the two domains. In unphosphorylated CheB, the N-terminal domain packs against the active site of the C-terminal domain and thus inhibits methylesterase activity by directly restricting access to the active site. We propose that phosphorylation of CheB induces a conformational change in the regulatory domain that disrupts the domain interface, resulting in a repositioning of the domains and allowing access to the active site. Structural similarity between the two companion receptor modification enzymes, CheB and CheR, suggests an evolutionary and/or functional relationship. Specifically, the phosphorylated N-terminal domain of CheB may facilitate interaction with the receptors, similar to the postulated role of the N-terminal domain of CheR. Examination of surfaces in the N-terminal regulatory domain of CheB suggests that despite a common fold throughout the response regulator family, surfaces used for protein-protein interactions differ significantly. Comparison between CheB and other response regulators indicates that analogous surfaces are used for different functions and conversely, similar functions are mediated by different molecular surfaces.
-===STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN===
+Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain.,Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1381-6. PMID:9465023<ref>PMID:9465023</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1a2o" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9465023}}, adds the Publication Abstract to the page
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9465023 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9465023}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-A2O 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=1A2O OCA].
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
+[[Category: Djordjevic S]]
-==Reference==
+[[Category: Goudreau PN]]
-Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain., Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH, Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1381-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9465023 9465023]
+[[Category: Stock AM]]
-[[Category: Protein-glutamate methylesterase]]
+[[Category: West AH]]
-[[Category: Salmonella typhimurium]]
+[[Category: Xu Q]]
-[[Category: Single protein]]
-[[Category: Djordjevic, S.]]
-[[Category: Goudreau, P N.]]
-[[Category: Stock, A M.]]
-[[Category: West, A H.]]
-[[Category: Xu, Q.]]
-[[Category: Adaptation]]
-[[Category: Bacterial chemotaxis]]
-[[Category: Serine hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:52:02 2008''