1chd

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[[Image:1chd.jpg|left|200px]]
 
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{{Structure
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==CHEB METHYLESTERASE DOMAIN==
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|PDB= 1chd |SIZE=350|CAPTION= <scene name='initialview01'>1chd</scene>, resolution 1.75&Aring;
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<StructureSection load='1chd' size='340' side='right'caption='[[1chd]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= [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]
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</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>
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|GENE= CHEB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium])
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<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>
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}}
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/1chd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1chd ConSurf].
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<div style="clear:both"></div>
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'''CHEB METHYLESTERASE DOMAIN'''
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==See Also==
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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==About this Structure==
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[[Category: Martinez-Hackert E]]
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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].
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[[Category: Stock AM]]
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[[Category: West AH]]
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==Reference==
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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]
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[[Category: Protein-glutamate methylesterase]]
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[[Category: Salmonella typhimurium]]
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[[Category: Single protein]]
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[[Category: Martinez-Hackert, E.]]
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[[Category: Stock, A M.]]
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[[Category: West, A H.]]
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[[Category: chemotaxis protein]]
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[[Category: serine hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:28 2008''
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Current revision

CHEB METHYLESTERASE DOMAIN

PDB ID 1chd

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