1rzs

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(New page: 200px<br /><applet load="1rzs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzs" /> '''Solution structure of P22 Cro'''<br /> ==Ov...)
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[[Image:1rzs.gif|left|200px]]<br /><applet load="1rzs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rzs" />
 
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'''Solution structure of P22 Cro'''<br />
 
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==Overview==
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==Solution structure of P22 Cro==
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We report the solution structure of the Cro protein from bacteriophage, P22. Comparisons of its sequence and structure to those of lambda Cro, strongly suggest an alpha-to-beta secondary structure switching event, during Cro evolution. The folds of P22 Cro and lambda Cro share a three, alpha helix fragment comprising the N-terminal half of the domain., However, P22 Cro's C terminus folds as two helices, while lambda Cro's, folds as a beta hairpin. The all-alpha fold found for P22 Cro appears to, be ancestral, since it also occurs in cI proteins, which are anciently, duplicated paralogues of Cro. PSI-BLAST and transitive homology analyses, strongly suggest that the sequences of P22 Cro and lambda Cro are globally, homologous despite encoding different folds. The alpha+beta fold of lambda, Cro therefore likely evolved from its all-alpha ancestor by homologous, secondary structure switching, rather than by nonhomologous replacement of, both sequence and structure.
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<StructureSection load='1rzs' size='340' side='right'caption='[[1rzs]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rzs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZS 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">Solution NMR</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=1rzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzs OCA], [https://pdbe.org/1rzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzs RCSB], [https://www.ebi.ac.uk/pdbsum/1rzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RCRO_BPP22 RCRO_BPP22] Cro represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operators regions normally used by the repressor protein for lysogenic maintenance.
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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/rz/1rzs_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=1rzs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We report the solution structure of the Cro protein from bacteriophage P22. Comparisons of its sequence and structure to those of lambda Cro strongly suggest an alpha-to-beta secondary structure switching event during Cro evolution. The folds of P22 Cro and lambda Cro share a three alpha helix fragment comprising the N-terminal half of the domain. However, P22 Cro's C terminus folds as two helices, while lambda Cro's folds as a beta hairpin. The all-alpha fold found for P22 Cro appears to be ancestral, since it also occurs in cI proteins, which are anciently duplicated paralogues of Cro. PSI-BLAST and transitive homology analyses strongly suggest that the sequences of P22 Cro and lambda Cro are globally homologous despite encoding different folds. The alpha+beta fold of lambda Cro therefore likely evolved from its all-alpha ancestor by homologous secondary structure switching, rather than by nonhomologous replacement of both sequence and structure.
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==About this Structure==
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Secondary structure switching in Cro protein evolution.,Newlove T, Konieczka JH, Cordes MH Structure. 2004 Apr;12(4):569-81. PMID:15062080<ref>PMID:15062080</ref>
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1RZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RZS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Secondary structure switching in Cro protein evolution., Newlove T, Konieczka JH, Cordes MH, Structure. 2004 Apr;12(4):569-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15062080 15062080]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1rzs" style="background-color:#fffaf0;"></div>
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[[Category: Yersinia phage py54]]
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== References ==
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[[Category: Cordes, M.H.]]
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<references/>
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[[Category: Konieczka, J.H.]]
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__TOC__
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[[Category: Newlove, T.]]
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</StructureSection>
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[[Category: dna-binding protein]]
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[[Category: Large Structures]]
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[[Category: helix-turn-helix]]
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[[Category: Salmonella virus P22]]
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[[Category: structural evolution]]
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[[Category: Cordes MH]]
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[[Category: Konieczka JH]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:59:21 2007''
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[[Category: Newlove T]]

Current revision

Solution structure of P22 Cro

PDB ID 1rzs

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