1vls

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(New page: 200px<br /><applet load="1vls" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vls, resolution 1.85&Aring;" /> '''LIGAND BINDING DOMAI...)
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[[Image:1vls.gif|left|200px]]<br /><applet load="1vls" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vls, resolution 1.85&Aring;" />
 
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'''LIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR'''<br />
 
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==Overview==
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==LIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR==
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The high-resolution structures of the wild-type periplasmic domain of the, bacterial aspartate receptor have been determined in the absence and, presence of bound aspartate to 1.85 and 2.2 A resolution, respectively. As, we reported earlier, in the refined structure of the complexed form of the, crosslinked cysteine mutant receptor, the binding of the aspartate at the, first site was mediated through four bridging water molecules while the, second site showed an occupant electron density that best fit a sulfate, group, which was present in the crystallization solution at high, concentration. In the wild-type periplasmic domain structure two aspartate, residues are bound per dimer, but with different occupancies. There exists, a "strong" aspartate-binding site whose binding is again mediated by four, water molecules while the second site contains aspartate whose B-factor is, about 10% higher, signifying weaker binding. The interaction between the, second, "weaker" aspartate with the three ligand-binding arginine, side-chains is slightly different from the first site. The major, difference is that there are three water molecules mediating the binding, of aspartate at the second site, whereas in the first site there are four, bridging water molecules. The fact that aspartate-complexed crystals of, the wild-type were grown with a large excess aspartate while the, cross-linked crystals were grown with equal molar aspartate may explain, the difference in the stoichiometry observed. The conservation of the four, bridging water molecules in the strong aspartate site of both the, cross-linked and wild-type periplasmic domain may reflect an important, binding motif. The periplasmic domain in the apo form is a symmetrical, dimer, in which each of the subunits is equivalent, and the two aspartate, binding sites are identical. Upon the binding of aspartate, the subunits, are no longer symmetrical. The main difference between the aspartate-bound, and unbound forms is in a small, rigid-body rotation between the subunits, within a dimer. The rotation is similar in both direction and magnitude in, the crosslinked and wild-type periplasmic domains. The presence of the, second aspartate in the wild-type structure does not make any additional, rotation compared to the single-site binding. The conservation of the, small angular change in vitro suggests that the inter-subunit rotation may, have relevance to the understanding of the mechanism of transmembrane, signal transduction in vivo.
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<StructureSection load='1vls' size='340' side='right'caption='[[1vls]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vls]] 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=1VLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLS 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]] 1.85&#8491;</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=1vls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vls OCA], [https://pdbe.org/1vls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vls RCSB], [https://www.ebi.ac.uk/pdbsum/1vls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vls ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MCP2_SALTY MCP2_SALTY] Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis. 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/vl/1vls_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=1vls 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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1VLS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VLS 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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High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor., Yeh JI, Biemann HP, Prive GG, Pandit J, Koshland DE Jr, Kim SH, J Mol Biol. 1996 Sep 20;262(2):186-201. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8831788 8831788]
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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: Biemann H-P]]
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[[Category: Biemann, H.P.]]
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[[Category: Kim S-H]]
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[[Category: Junior, D.E.Koshland.]]
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[[Category: Koshland Junior DE]]
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[[Category: Kim, S.H.]]
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[[Category: Pandit J]]
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[[Category: Pandit, J.]]
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[[Category: Prive G]]
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[[Category: Prive, G.]]
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[[Category: Yeh JI]]
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[[Category: Yeh, J.I.]]
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[[Category: bacterial chemotaxis receptor]]
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[[Category: chemotaxis]]
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[[Category: unbound]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:56:40 2007''
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Current revision

LIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR

PDB ID 1vls

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