1rpo

<table><tr><td colspan='2'>[[1rpo]] is a 1 chain structure with sequence from [https://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=1RPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPO 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=1rpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rpo OCA], [https://pdbe.org/1rpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rpo RCSB], [https://www.ebi.ac.uk/pdbsum/1rpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rpo ProSAT]</span></td></tr>

[[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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== Publication Abstract from PubMed ==

The sequences of alpha-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frequently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour. Thus, formation of alpha-alpha-hairpin bends may occur both in the presence and absence of heptad breaks.

Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle.,Vlassi M, Steif C, Weber P, Tsernoglou D, Wilson KS, Hinz HJ, Kokkinidis M Nat Struct Biol. 1994 Oct;1(10):706-16. PMID:7634075<ref>PMID:7634075</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Kokkinidis, M]]

[[Category: Vlassi, M]]

[[Category: Transcription regulation]]