4do2

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==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==
==Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.==
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<StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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<StructureSection load='4do2' size='340' side='right'caption='[[4do2]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4do2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4do2]] 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=4DO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DO2 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]]</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]] 1.401&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rop ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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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=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [https://pdbe.org/4do2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [https://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4do2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [http://www.ebi.ac.uk/pdbsum/4do2 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region has attracted considerable interest because a single alanine-to-proline substitution (A31P) in the loop is sufficient to change the topology of this small protein. In order to further analyse the loop region as a possible folding-control element, the double mutant D30P/A31G (RopPG) was produced, purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and two molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 1.4 A using synchrotron radiation.
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Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.,Ambrazi M, Fellas G, Kapetaniou EG, Kotsifaki D, Providaki M, Kokkinidis M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):432-4. doi:, 10.1107/S1744309108011342. Epub 2008 Apr 30. PMID:18453719<ref>PMID:18453719</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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==See Also==
==See Also==
*[[Rop protein|Rop protein]]
*[[Rop protein|Rop protein]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Amprazi, M]]
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[[Category: Large Structures]]
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[[Category: Kapetaniou, E G]]
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[[Category: Amprazi M]]
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[[Category: M., Kokkinidis]]
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[[Category: Kapetaniou EG]]
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[[Category: 4-alpha-helical bundle]]
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[[Category: Kokkinidis M]]
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[[Category: Bacterial protein]]
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[[Category: Cole1 plasmid copy number]]
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[[Category: Loop]]
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[[Category: Mutation]]
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[[Category: Protein folding]]
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[[Category: Protein structure]]
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[[Category: Rna binding protein]]
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[[Category: Rop protein]]
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Current revision

Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.

PDB ID 4do2

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