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[[Image:1jmw.jpg|left|200px]]<br /><applet load="1jmw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jmw, resolution 1.9&Aring;" />
'''Propagating Conformational Changes Over Long (And Short) Distances'''<br />


==Overview==
==Propagating Conformational Changes Over Long (And Short) Distances==
The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.
<StructureSection load='1jmw' size='340' side='right'caption='[[1jmw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jmw]] 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=1JMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMW 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]] 1.9&#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=1jmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmw OCA], [https://pdbe.org/1jmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmw RCSB], [https://www.ebi.ac.uk/pdbsum/1jmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmw 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/jm/1jmw_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=1jmw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1JMW 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMW OCA].
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
==Reference==
__TOC__
Propagating conformational changes over long (and short) distances in proteins., Yu EW, Koshland DE Jr, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9517-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11504940 11504940]
</StructureSection>
[[Category: Salmonella typhimurium]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Jr., D E.Koshland.]]
[[Category: Koshland Jr DE]]
[[Category: Yu, E W.]]
[[Category: Yu EW]]
[[Category: bacterial chemotactic receptor]]
[[Category: chemotaxis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:25 2008''

Latest revision as of 10:40, 7 February 2024

Propagating Conformational Changes Over Long (And Short) DistancesPropagating Conformational Changes Over Long (And Short) Distances

Structural highlights

1jmw 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 1.9Å
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

1jmw, resolution 1.90Å

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