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1omh

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(New page: 200px<br /><applet load="1omh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omh, resolution 1.95&Aring;" /> '''Conjugative Relaxase...)
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[[Image:1omh.gif|left|200px]]<br /><applet load="1omh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1omh, resolution 1.95&Aring;" />
 
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'''Conjugative Relaxase TrwC in complex with OriT Dna. Metal-free structure.'''<br />
 
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==Overview==
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==Conjugative Relaxase TrwC in complex with OriT Dna. Metal-free structure.==
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Relaxases are DNA strand transferases that catalyze the initial and final, stages of DNA processing during conjugative cell-to-cell DNA transfer., Upon binding to the origin of transfer (oriT) DNA, relaxase TrwC melts the, double helix. The three-dimensional structure of the relaxase domain of, TrwC in complex with its cognate DNA at oriT shows a fold built on a, two-layer alpha/beta sandwich, with a deep narrow cleft that houses the, active site. The DNA includes one arm of an extruded cruciform, an, essential feature for specific recognition. This arm is firmly embraced by, the protein through a beta-ribbon positioned in the DNA major groove and a, loop occupying the minor groove. It is followed by a single-stranded DNA, segment that enters the active site, after a sharp U-turn forming a, hydrophobic cage that traps the N-terminal methionine. Structural analysis, combined with site-directed mutagenesis defines the architecture of the, active site.
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<StructureSection load='1omh' size='340' side='right'caption='[[1omh]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1omh]] 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=1OMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMH FirstGlance]. <br>
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1OMH 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OMH OCA].
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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]] 1.95&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1omh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omh OCA], [https://pdbe.org/1omh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omh RCSB], [https://www.ebi.ac.uk/pdbsum/1omh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omh ProSAT]</span></td></tr>
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Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC., Guasch A, Lucas M, Moncalian G, Cabezas M, Perez-Luque R, Gomis-Ruth FX, de la Cruz F, Coll M, Nat Struct Biol. 2003 Dec;10(12):1002-10. Epub 2003 Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14625590 14625590]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q47673_ECOLX Q47673_ECOLX]
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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/om/1omh_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=1omh ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cabezas, M.]]
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[[Category: Cabezas M]]
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[[Category: Coll, M.]]
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[[Category: Coll M]]
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[[Category: Cruz, F.de.la.]]
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[[Category: Gomis-Ruth FX]]
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[[Category: Gomis-Ruth, F.X.]]
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[[Category: Guasch A]]
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[[Category: Guasch, A.]]
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[[Category: Lucas M]]
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[[Category: Lucas, M.]]
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[[Category: Moncalian G]]
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[[Category: Moncalian, G.]]
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[[Category: Perez-Luque R]]
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[[Category: Perez-Luque, R.]]
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[[Category: De la Cruz F]]
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[[Category: SO4]]
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[[Category: bacterial conjugation]]
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[[Category: dna replication]]
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[[Category: protein-dna complex]]
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[[Category: relaxase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:05:55 2007''
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Current revision

Conjugative Relaxase TrwC in complex with OriT Dna. Metal-free structure.

PDB ID 1omh

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