1af7

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(New page: 200px<br /><applet load="1af7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1af7, resolution 2.0&Aring;" /> '''CHER FROM SALMONELLA ...)
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[[Image:1af7.gif|left|200px]]<br /><applet load="1af7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1af7, resolution 2.0&Aring;" />
 
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'''CHER FROM SALMONELLA TYPHIMURIUM'''<br />
 
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==Overview==
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==CHER FROM SALMONELLA TYPHIMURIUM==
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BACKGROUND: Flagellated bacteria swim towards favorable chemicals and away, from deleterious ones. The sensing of chemoeffector gradients involves, chemotaxis receptors, transmembrane proteins that detect stimuli through, their periplasmic domains and transduce signals via their cytoplasmic, domains to the downstream signaling components. Signaling outputs from, chemotaxis receptors are influenced both by the binding of the, chemoeffector ligand to the periplasmic domain and by methylation of, specific glutamate residues on the cytoplasmic domain of the receptor., Methylation is catalyzed by CheR, an S-adenosylmethionine-dependent, methyltransferase. CheR forms a tight complex with the receptor by binding, a region of the receptors that is distinct from the methylation site. CheR, belongs to a broad class of enzymes involved in the methylation of a, variety of substrates. Until now, no structure from the class of protein, methyltransferases has been characterized. RESULTS: The structure of the, Salmonella typhimurium chemotaxis receptor methyltransferase CheR bound to, S-adenosylhomocysteine, a product and inhibitor of the methylation, reaction, has been determined at 2.0 A resolution. The structure reveals, CheR to be a two-domain protein, with a smaller N-terminal helical domain, linked through a single polypeptide connection to a larger C-terminal, alpha/beta domain. The C-terminal domain has the characteristics of a, nucleotide-binding fold, with an insertion of a small antiparallel beta, sheet subdomain. The S-adenosylhomocysteine-binding site is formed mainly, by the large domain, with contributions from residues within the, N-terminal domain and the linker region. CONCLUSIONS: The CheR structure, shares some structural similarities with small molecule DNA and RNA, methyltransferases, despite a lack of sequence similarity among them. In, particular, there is significant structural preservation of the, S-adenosylmethionine-binding clefts; the specific length and conformation, of a loop in the alpha/beta domain seems to be required for, S-adenosylmethionine binding within these enzymes. Unique structural, features of CheR, such as the beta subdomain, are probably necessary for, CheR's specific interaction with its substrates, the bacterial chemotaxis, receptors.
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<StructureSection load='1af7' size='340' side='right'caption='[[1af7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1af7]] 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=1AF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AF7 FirstGlance]. <br>
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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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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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=1af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af7 OCA], [https://pdbe.org/1af7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1af7 RCSB], [https://www.ebi.ac.uk/pdbsum/1af7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1af7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHER_SALTY CHER_SALTY] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
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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/af/1af7_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=1af7 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AF7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AF7 OCA].
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
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==Reference==
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__TOC__
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Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine., Djordjevic S, Stock AM, Structure. 1997 Apr 15;5(4):545-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9115443 9115443]
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</StructureSection>
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[[Category: Protein-glutamate O-methyltransferase]]
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[[Category: Large Structures]]
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[[Category: Salmonella typhimurium]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Single protein]]
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[[Category: Djordjevic S]]
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[[Category: Djordjevic, S.]]
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[[Category: Stock AM]]
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[[Category: Stock, A.M.]]
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[[Category: SAH]]
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[[Category: chemotaxis receptor methylation]]
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[[Category: methyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:48:31 2007''
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Current revision

CHER FROM SALMONELLA TYPHIMURIUM

PDB ID 1af7

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