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New page: left|200px<br /><applet load="1cmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmc, resolution 1.8Å" /> '''THREE DIMENSIONAL CRY...
 
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[[Image:1cmc.gif|left|200px]]<br /><applet load="1cmc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cmc, resolution 1.8&Aring;" />
'''THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR'''<br />


==Overview==
==THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR==
The three-dimensional crystal structure of met repressor, in the presence, or absence of bound corepressor (S-adenosylmethionine), shows a dimer of, intertwined monomers, which do not have the helix-turn-helix motif, characteristic of other bacterial repressor and activator structures. We, propose that the interaction of met repressor with DNA occurs through, either a pair of symmetry-related alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions.
<StructureSection load='1cmc' size='340' side='right'caption='[[1cmc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cmc]] is a 2 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=1CMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMC 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=1cmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmc OCA], [https://pdbe.org/1cmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmc RCSB], [https://www.ebi.ac.uk/pdbsum/1cmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METJ_ECOLI METJ_ECOLI] This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.[HAMAP-Rule:MF_00744]
== 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/cm/1cmc_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=1cmc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CMC 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 MG and SAM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMC OCA].
*[[Met repressor|Met repressor]]
 
__TOC__
==Reference==
</StructureSection>
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor., Rafferty JB, Somers WS, Saint-Girons I, Phillips SE, Nature. 1989 Oct 26;341(6244):705-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2677753 2677753]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Phillips, S.E.V.]]
[[Category: Phillips SEV]]
[[Category: Somers, W.S.]]
[[Category: Somers WS]]
[[Category: MG]]
[[Category: SAM]]
[[Category: dna-binding regulatory protein]]
 
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