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==THE STRUCTURE OF COLE1 ROP IN SOLUTION==
==THE STRUCTURE OF COLE1 ROP IN SOLUTION==
<StructureSection load='1rpr' size='340' side='right'caption='[[1rpr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1rpr' size='340' side='right'caption='[[1rpr]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1rpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1rpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPR FirstGlance]. <br>
</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=1rpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpr OCA], [https://pdbe.org/1rpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rpr RCSB], [https://www.ebi.ac.uk/pdbsum/1rpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpr ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1rpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpr OCA], [https://pdbe.org/1rpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rpr RCSB], [https://www.ebi.ac.uk/pdbsum/1rpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX]] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.  
[https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.
== 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=1rpr 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=1rpr ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces appear to influence the crystal structure.
The structure of ColE1 rop in solution.,Eberle W, Pastore A, Sander C, Rosch P J Biomol NMR. 1991 May;1(1):71-82. PMID:1841691<ref>PMID:1841691</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1rpr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Rop protein|Rop protein]]
*[[Rop protein|Rop protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eberle, W]]
[[Category: Eberle W]]
[[Category: Klaus, W]]
[[Category: Klaus W]]
[[Category: Pastore, A]]
[[Category: Pastore A]]
[[Category: Roesch, P]]
[[Category: Roesch P]]
[[Category: Sander, C]]
[[Category: Sander C]]
[[Category: Transcription regulation]]

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