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New page: left|200px<br /><applet load="1was" size="450" color="white" frame="true" align="right" spinBox="true" caption="1was, resolution 2.7Å" /> '''THE THREE-DIMENSIONAL...
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR'''<br />


==Overview==
==THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR==
The three-dimensional structures of the ligand-binding domain of the, wild-type Salmonella typhimurium aspartate receptor have been determined, in the absence (apo) and presence of bound aspartate (complex) and, compared to a cross-linked mutant containing a cysteine at position 36, which does not change signaling behavior of the intact receptor. The, structures of the wild-type forms were determined in order to assess the, effects of cross-linking on the structure and its influence on, conformational changes upon ligand binding. As in the case of the, cross-linked mutant receptor, the non-cross-linked ligand-binding domain, is dimeric and is composed of 4-alpha-helical bundle monomer subunits, related by a crystallographic 2-fold axis in the unbound form and by a, non-crystallographic axis in the aspartate-bound form. A comparative study, between the non-cross-linked and cross-linked structures has led to the, following observations: 1) The long N-terminal helices of the individual, subunits in the cross-linked structures are bent toward each other to, accommodate the disulfide bond. 2) The rest of the subunit conformation is, very similar to that of the wild-type. 3) The intersubunit angle of the, cross-linked apo structure is larger by about 13 degrees when compared to, the wild-type apo structure. 4) The nature and magnitude of the, aspartate-induced conformational changes in the non-cross-linked wild-type, structures are very similar to those of the cross-linked structures.
<StructureSection load='1was' size='340' side='right'caption='[[1was]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1was]] 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=1WAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1was FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1was OCA], [https://pdbe.org/1was PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1was RCSB], [https://www.ebi.ac.uk/pdbsum/1was PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1was ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1was_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1was ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1WAS 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=1WAS OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding., Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH, J Biol Chem. 1993 May 5;268(13):9787-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8486661 8486661]
[[Category: Large Structures]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Single protein]]
[[Category: Kim S-H]]
[[Category: Kim, S.H.]]
[[Category: chemotaxis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:17:06 2007''

Latest revision as of 11:47, 14 February 2024

THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTORTHE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR

Structural highlights

1was is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1was, resolution 2.70Å

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