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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.== |
| - | <StructureSection load='4do2' size='340' side='right' caption='[[4do2]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='4do2' size='340' side='right'caption='[[4do2]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4do2]] is a 2 chain structure with sequence from [http://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=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> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rop|1rop]]</td></tr> | + | </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=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> |
| - | <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 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <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://pdbe.org/4do2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4do2 RCSB], [http://www.ebi.ac.uk/pdbsum/4do2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4do2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [[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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Amprazi, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Kapetaniou, E G]] | + | [[Category: Amprazi M]] |
| - | [[Category: Kokkinidis, M]]
| + | [[Category: Kapetaniou EG]] |
| - | [[Category: 4-alpha-helical bundle]] | + | [[Category: Kokkinidis M]] |
| - | [[Category: Bacterial protein]] | + | |
| - | [[Category: Cole1 plasmid copy number]]
| + | |
| - | [[Category: Loop]]
| + | |
| - | [[Category: Mutation]]
| + | |
| - | [[Category: Protein folding]]
| + | |
| - | [[Category: Protein structure]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rop protein]]
| + | |
| Structural highlights
Function
[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.
Publication Abstract from PubMed
The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-alpha-helical bundles, is characterized by a remarkable structural plasticity. Loop region mutations lead to a wide range of topologies, folding states, and altered physicochemical properties. A protein-folding study of Rop and several loop variants has identified specific residues and sequences that are linked to the observed structural plasticity. Apart from the native state, native-like and molten-globule states have been identified; these states are sensitive to reducing agents due to the formation of nonnative disulfide bridges. Pro residues in the loop are critical for the establishment of new topologies and molten globule states; their effects, however, can be in part compensated by Gly residues. The extreme plasticity in the assembly of 4-alpha-helical bundles reflects the capacity of the Rop sequence to combine a specific set of hydrophobic residues into strikingly different hydrophobic cores. These cores include highly hydrated ones that are consistent with the formation of interchain, nonnative disulfide bridges and the establishment of molten globules. Potential applications of this structural plasticity are among others in the engineering of bio-inspired materials.
Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.,Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Perez J, Kokkinidis M Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11049-54. doi:, 10.1073/pnas.1322065111. Epub 2014 Jul 14. PMID:25024213[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Perez J, Kokkinidis M. Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein. Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11049-54. doi:, 10.1073/pnas.1322065111. Epub 2014 Jul 14. PMID:25024213 doi:http://dx.doi.org/10.1073/pnas.1322065111
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