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1rpo

From Proteopedia

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(New page: 200px<br /><applet load="1rpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpo, resolution 1.4&Aring;" /> '''RESTORED HEPTAD PATTE...)
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[[Image:1rpo.jpg|left|200px]]<br /><applet load="1rpo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rpo, resolution 1.4&Aring;" />
 
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'''RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE'''<br />
 
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==Overview==
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==RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE==
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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.
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<StructureSection load='1rpo' size='340' side='right'caption='[[1rpo]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rpo]] is a 1 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=1RPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RPO FirstGlance]. <br>
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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]] 1.4&#8491;</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=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>
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rp/1rpo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1rpo ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1RPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RPO OCA].
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*[[Rop protein|Rop protein]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7634075 7634075]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kokkinidis, M.]]
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[[Category: Kokkinidis M]]
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[[Category: Vlassi, M.]]
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[[Category: Vlassi M]]
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[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:46:43 2007''
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Current revision

RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE

PDB ID 1rpo

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