2asr

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(New page: 200px<br /><applet load="2asr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2asr, resolution 2.3&Aring;" /> '''THE THREE-DIMENSIONAL...)
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[[Image:2asr.jpg|left|200px]]<br /><applet load="2asr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2asr, resolution 2.3&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI==
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The crystal structure of the periplasmic domain of the aspartate receptor, from Escherichia coli has been solved and refined to an R-factor of 0.203, at 2.3 A, resolution. The dimeric protein is largely helical, with four, helices from each monomer forming a four-helix bundle. The dimer interface, is constructed from four helices, two from each subunit, also packed, together in a four-helix bundle arrangement. A sulfate ion occupies the, aspartate-binding site. All hydrogen bonds made to aspartate are, substituted by direct or water-mediated hydrogen bonds to the sulfate., Comparison of the Escherichia coli aspartate-receptor structure with that, of Salmonella typhimurium [Milburn, Prive, Milligan, Scott, Yeh, Jancarik, Koshland &amp; Kim (1991). Science, 254, 1342-1347; Scott, Milligan, Milburn, Prive, Yeh, Koshland &amp; Kim (1993). J. Mol. Biol. 232, 555-573] reveals, strong conservation in the structure of the monomer, but more divergence, in the orientation of the subunits with respect to one another. Mutations, that render the Escherichia coli receptor incapable of responding to, maltose are either located in spatially conserved sites or in regions of, the structures that have high temperature factors and are therefore likely, to be quite flexible. The inability of the receptor from Salmonella, typhimurium to respond to maltose may, therefore, be because of, differences in amino acids located on the binding surface rather than, structural differences.
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<StructureSection load='2asr' size='340' side='right'caption='[[2asr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2asr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ASR 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]] 2.3&#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=SO4:SULFATE+ION'>SO4</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=2asr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asr OCA], [https://pdbe.org/2asr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2asr RCSB], [https://www.ebi.ac.uk/pdbsum/2asr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2asr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MCP2_ECOLI MCP2_ECOLI] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel. Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
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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/as/2asr_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=2asr 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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2ASR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ASR OCA].
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The three-dimensional structure of the aspartate receptor from Escherichia coli., Bowie JU, Pakula AA, Simon MI, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):145-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299315 15299315]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bowie, J.U.]]
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[[Category: Bowie JU]]
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[[Category: Pakula, A.A.]]
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[[Category: Pakula AA]]
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[[Category: Simon, M.I.]]
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[[Category: Simon MI]]
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[[Category: SO4]]
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[[Category: chemotaxis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:20:47 2007''
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THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTATE RECEPTOR FROM ESCHERICHIA COLI

PDB ID 2asr

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