1chd: Difference between revisions

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New page: left|200px<br /><applet load="1chd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chd, resolution 1.75Å" /> '''CHEB METHYLESTERASE ...
 
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[[Image:1chd.jpg|left|200px]]<br /><applet load="1chd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1chd, resolution 1.75&Aring;" />
'''CHEB METHYLESTERASE DOMAIN'''<br />


==Overview==
==CHEB METHYLESTERASE DOMAIN==
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.
<StructureSection load='1chd' size='340' side='right'caption='[[1chd]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
</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>


==About this Structure==
==See Also==
1CHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Active as [http://en.wikipedia.org/wiki/Protein-glutamate_methylesterase Protein-glutamate methylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.61 3.1.1.61] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CHD OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7608974 7608974]
[[Category: Large Structures]]
[[Category: Protein-glutamate methylesterase]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Salmonella typhimurium]]
[[Category: Martinez-Hackert E]]
[[Category: Single protein]]
[[Category: Stock AM]]
[[Category: Martinez-Hackert, E.]]
[[Category: West AH]]
[[Category: Stock, A.M.]]
[[Category: West, A.H.]]
[[Category: chemotaxis protein]]
[[Category: serine hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:27:26 2007''

Latest revision as of 06:43, 7 February 2024

CHEB METHYLESTERASE DOMAIN

1chd, resolution 1.75Å

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