1bc5

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[[Image:1bc5.gif|left|200px]]<br />
 
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<applet load="1bc5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bc5, resolution 2.2&Aring;" />
 
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'''CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER'''<br />
 
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==Overview==
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==CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER==
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Signal transduction processes commonly involve reversible covalent, modifications of receptors. Bacterial chemotaxis receptors are reversibly, methylated at specific glutamate residues within coiled-coil regions of, their cytoplasmic domains. Methylation is catalyzed by an, S-adenosylmethionine-dependent protein methyltransferase, CheR, that binds, to a specific sequence at the C-termini of some chemotaxis receptors. From, this tethering point, CheR methylates neighboring receptor molecules. We, report the crystal structure, determined to 2.2 A resolution, of a complex, of the Salmonella typhimurium methyltransferase CheR bound to the, methylation reaction product, S-adenosylhomocysteine (AdoHcy), and the, C-terminal pentapeptide of the aspartate receptor, Tar. The structure, indicates the basis for the specificity of interaction between the, chemoreceptors and CheR and identifies a specific receptor binding motif, incorporated in the CheR methyltransferase domain.
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<StructureSection load='1bc5' size='340' side='right'caption='[[1bc5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bc5]] 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=1BC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC5 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]] 2.2&#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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <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=1bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc5 OCA], [https://pdbe.org/1bc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc5 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/bc/1bc5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bc5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Signal transduction processes commonly involve reversible covalent modifications of receptors. Bacterial chemotaxis receptors are reversibly methylated at specific glutamate residues within coiled-coil regions of their cytoplasmic domains. Methylation is catalyzed by an S-adenosylmethionine-dependent protein methyltransferase, CheR, that binds to a specific sequence at the C-termini of some chemotaxis receptors. From this tethering point, CheR methylates neighboring receptor molecules. We report the crystal structure, determined to 2.2 A resolution, of a complex of the Salmonella typhimurium methyltransferase CheR bound to the methylation reaction product, S-adenosylhomocysteine (AdoHcy), and the C-terminal pentapeptide of the aspartate receptor, Tar. The structure indicates the basis for the specificity of interaction between the chemoreceptors and CheR and identifies a specific receptor binding motif incorporated in the CheR methyltransferase domain.
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==About this Structure==
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Chemotaxis receptor recognition by protein methyltransferase CheR.,Djordjevic S, Stock AM Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482<ref>PMID:9628482</ref>
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1BC5 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 CO, ACE and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Structure known Active Site: COB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Chemotaxis receptor recognition by protein methyltransferase CheR., Djordjevic S, Stock AM, Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9628482 9628482]
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</div>
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[[Category: Protein-glutamate O-methyltransferase]]
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<div class="pdbe-citations 1bc5" style="background-color:#fffaf0;"></div>
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[[Category: Salmonella typhimurium]]
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[[Category: Single protein]]
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[[Category: Djordjevic, S.]]
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[[Category: Stock, A.M.]]
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[[Category: ACE]]
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[[Category: CO]]
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[[Category: SAH]]
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[[Category: chemotaxis receptor]]
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[[Category: complex (methyltransferase/peptide)]]
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[[Category: methyltransferase]]
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[[Category: peptide binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:54:05 2007''
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==See Also==
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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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Djordjevic S]]
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[[Category: Stock AM]]

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CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER

PDB ID 1bc5

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