1cmb

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Current revision (06:43, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1cmb' size='340' side='right'caption='[[1cmb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1cmb' size='340' side='right'caption='[[1cmb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1cmb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1cmb]] 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=1CMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 1.8&#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=PO4:PHOSPHATE+ION'>PO4</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=1cmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmb OCA], [https://pdbe.org/1cmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmb RCSB], [https://www.ebi.ac.uk/pdbsum/1cmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmb ProSAT]</span></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=1cmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmb OCA], [https://pdbe.org/1cmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmb RCSB], [https://www.ebi.ac.uk/pdbsum/1cmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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]
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1cmb ConSurf].
</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=1cmb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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:2677753<ref>PMID:2677753</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1cmb" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Met repressor|Met repressor]]
*[[Met repressor|Met repressor]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phillips, K]]
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[[Category: Phillips K]]
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[[Category: Phillips, S E.V]]
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[[Category: Phillips SEV]]
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[[Category: Rafferty, J B]]
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[[Category: Rafferty JB]]
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[[Category: Dna-binding regulatory protein]]
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Current revision

THREE DIMENSIONAL CRYSTAL STRUCTURES OF ESCHERICHIA COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR

PDB ID 1cmb

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