1lrr

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(New page: 200px<br /><applet load="1lrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lrr, resolution 2.65&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1lrr.gif|left|200px]]<br /><applet load="1lrr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lrr, resolution 2.65&Aring;" />
 
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'''CRYSTAL STRUCTURE OF E. COLI SEQA COMPLEXED WITH HEMIMETHYLATED DNA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF E. COLI SEQA COMPLEXED WITH HEMIMETHYLATED DNA==
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The SeqA protein binds clusters of fully methylated or hemimethylated GATC, sequences at oriC and negatively modulates the initiation of DNA, replication. We find that SeqA can be proteolytically cleaved into an, N-terminal multimerization and a C-terminal DNA-binding domain and have, determined the crystal structure of the C-terminal domain in complex with, a hemimethylated GATC site. SeqA makes direct hydrogen bonds and van der, Waals contacts with the hemimethylated A-T base pair in addition to, interactions with the surrounding bases and DNA backbone. The tetrameric, protein-DNA complex found in the crystal suggests that SeqA binds multiple, GATC sites on separate DNA duplexes, altering the overall DNA topology and, sequestering oriC from replication initiation.
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<StructureSection load='1lrr' size='340' side='right'caption='[[1lrr]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lrr]] is a 6 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=1LRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LRR FirstGlance]. <br>
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1LRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LRR 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]] 2.65&#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=6MA:N6-METHYL-DEOXY-ADENOSINE-5-MONOPHOSPHATE'>6MA</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=1lrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lrr OCA], [https://pdbe.org/1lrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lrr RCSB], [https://www.ebi.ac.uk/pdbsum/1lrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lrr ProSAT]</span></td></tr>
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Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex., Guarne A, Zhao Q, Ghirlando R, Yang W, Nat Struct Biol. 2002 Nov;9(11):839-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12379844 12379844]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SEQA_ECOLI SEQA_ECOLI] Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. Can also bind to hemimethylated GATC sequences outside of oriC region. Binds, with less affinity, to fully methylated GATC sites and affects timing of replication. May play a role in chromosome organization and gene regulation.<ref>PMID:8011018</ref> <ref>PMID:7891562</ref> <ref>PMID:7553853</ref> <ref>PMID:11080170</ref> <ref>PMID:10931282</ref> <ref>PMID:20689753</ref>
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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/lr/1lrr_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=1lrr ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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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: Guarne, A.]]
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[[Category: Guarne A]]
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[[Category: Guirlando, R.]]
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[[Category: Guirlando R]]
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[[Category: Yang, W.]]
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[[Category: Yang W]]
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[[Category: Zhao, Q.]]
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[[Category: Zhao Q]]
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[[Category: methylated gatc]]
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[[Category: protein-dna complex]]
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[[Category: replication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:49:12 2007''
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Current revision

CRYSTAL STRUCTURE OF E. COLI SEQA COMPLEXED WITH HEMIMETHYLATED DNA

PDB ID 1lrr

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