4do2: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</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>
<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>
</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.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25024213</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4do2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Rop protein|Rop protein]]
*[[Rop protein|Rop protein]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 17:40, 14 March 2024

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.

Structural highlights

4do2 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.401Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

4do2, resolution 1.40Å

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