1chd: Difference between revisions

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[[Image:1chd.jpg|left|200px]]


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==CHEB METHYLESTERASE DOMAIN==
The line below this paragraph, containing "STRUCTURE_1chd", creates the "Structure Box" on the page.
<StructureSection load='1chd' size='340' side='right'caption='[[1chd]], [[Resolution|resolution]] 1.75&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'>[[1chd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHD 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]] 1.75&#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=1chd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chd OCA], [https://pdbe.org/1chd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chd RCSB], [https://www.ebi.ac.uk/pdbsum/1chd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chd ProSAT]</span></td></tr>
{{STRUCTURE_1chd| PDB=1chd |  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/ch/1chd_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=1chd ConSurf].
<div style="clear:both"></div>


'''CHEB METHYLESTERASE DOMAIN'''
==See Also==
 
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Signaling activity of bacterial chemotaxis transmembrane receptors is modulated by reversible covalent modification of specific receptor glutamate residues. The level of receptor methylation results from the activities of a specific S-adenosylmethionine-dependent methyltransferase, CheR, and the CheB methylesterase, which catalyzes hydrolysis of receptor glutamine or methylglutamate side-chains to glutamic acid. The CheB methylesterase belongs to a large family of response regulator proteins in which N-terminal regulatory domains control the activities of C-terminal effector domains. The crystal structure of the catalytic domain of the Salmonella typhimurium CheB methylesterase has been determined at 1.75 A resolution. The domain has a modified, doubly wound alpha/beta fold in which one of the helices is replaced by an anti-parallel beta-hairpin. Previous biochemical and mutagenesis data, suggest that the methylester hydrolysis catalyzed by CheB proceeds through a mechanism involving a serine nucleophile. The methylesterase active site is tentatively identified as a cleft at the C-terminal edge of the beta-sheet containing residues Ser164, His190 and Asp286. The three-dimensional fold, and the arrangement of residues within the catalytic triad distinguishes the CheB methylesterase from any previously described serine protease or serine hydrolase.
[[Category: Large Structures]]
 
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
==About this Structure==
[[Category: Martinez-Hackert E]]
1CHD 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=1CHD OCA].
[[Category: Stock AM]]
 
[[Category: West AH]]
==Reference==
Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB., West AH, Martinez-Hackert E, Stock AM, J Mol Biol. 1995 Jul 7;250(2):276-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7608974 7608974]
[[Category: Protein-glutamate methylesterase]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Martinez-Hackert, E.]]
[[Category: Stock, A M.]]
[[Category: West, A H.]]
[[Category: Chemotaxis protein]]
[[Category: Serine hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:44:04 2008''
Retrieved from "https://proteopedia.org/1chd"