1zae

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[[Image:1zae.gif|left|200px]]
 
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==Solution structure of the functional domain of phi29 replication organizer p16.7c==
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The line below this paragraph, containing "STRUCTURE_1zae", creates the "Structure Box" on the page.
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<StructureSection load='1zae' size='340' side='right'caption='[[1zae]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zae]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1z61 1z61]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZAE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=1zae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zae OCA], [https://pdbe.org/1zae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zae RCSB], [https://www.ebi.ac.uk/pdbsum/1zae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zae ProSAT]</span></td></tr>
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{{STRUCTURE_1zae| PDB=1zae | SCENE= }}
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</table>
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== Function ==
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'''Solution structure of the functional domain of phi29 replication organizer p16.7c'''
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[https://www.uniprot.org/uniprot/GP167_BPPH2 GP167_BPPH2] Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11169113, PubMed:11741949). Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid (PubMed:10921898). Required for the second pull step of DNA ejection (PubMed:17526715).<ref>PMID:10921898</ref> <ref>PMID:11169113</ref> <ref>PMID:11741949</ref> <ref>PMID:17526715</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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==Overview==
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The Bacillus subtilis phage phi29-encoded membrane protein p16.7 is one of the few proteins involved in prokaryotic membrane-associated DNA replication that has been characterized at a functional and biochemical level. In this work we have determined both the solution and crystal structures of its dimeric functional domain, p16.7C. Although the secondary structure of p16.7C is remarkably similar to that of the DNA binding homeodomain, present in proteins belonging to a large family of eukaryotic transcription factors, the tertiary structures of p16.7C and homeodomains are fundamentally different. In fact, p16.7C defines a novel dimeric six-helical fold. We also show that p16.7C can form multimers in solution and that this feature is a key factor for efficient DNA binding. Moreover, a combination of NMR and x-ray approaches, combined with functional analyses of mutants, revealed that multimerization of p16.7C dimers is mediated by a large protein surface that is characterized by a striking self-complementarity. Finally, the structural analyses of the p16.7C dimer and oligomers provide important clues about how protein multimerization and DNA binding are coupled.
The Bacillus subtilis phage phi29-encoded membrane protein p16.7 is one of the few proteins involved in prokaryotic membrane-associated DNA replication that has been characterized at a functional and biochemical level. In this work we have determined both the solution and crystal structures of its dimeric functional domain, p16.7C. Although the secondary structure of p16.7C is remarkably similar to that of the DNA binding homeodomain, present in proteins belonging to a large family of eukaryotic transcription factors, the tertiary structures of p16.7C and homeodomains are fundamentally different. In fact, p16.7C defines a novel dimeric six-helical fold. We also show that p16.7C can form multimers in solution and that this feature is a key factor for efficient DNA binding. Moreover, a combination of NMR and x-ray approaches, combined with functional analyses of mutants, revealed that multimerization of p16.7C dimers is mediated by a large protein surface that is characterized by a striking self-complementarity. Finally, the structural analyses of the p16.7C dimer and oligomers provide important clues about how protein multimerization and DNA binding are coupled.
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==About this Structure==
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Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding.,Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:15772069<ref>PMID:15772069</ref>
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1ZAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1z61 1z61]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAE 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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Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding., Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ, J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15772069 15772069]
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</div>
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[[Category: Bacillus phage phi29]]
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<div class="pdbe-citations 1zae" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Albert, A.]]
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<references/>
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[[Category: Asensio, J L.]]
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__TOC__
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[[Category: Gonzalez, C.]]
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</StructureSection>
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[[Category: Hermoso, J.]]
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[[Category: Bacillus virus phi29]]
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[[Category: Jimenez-Barbero, J.]]
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[[Category: Large Structures]]
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[[Category: Meijer, W J.J.]]
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[[Category: Albert A]]
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[[Category: Munoz-Espin, D.]]
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[[Category: Asensio JL]]
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[[Category: Salas, M.]]
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[[Category: Gonzalez C]]
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[[Category: Villar, L.]]
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[[Category: Hermoso J]]
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[[Category: Helical dimer]]
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[[Category: Jimenez-Barbero J]]
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[[Category: Nonspecific dna binding protein]]
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[[Category: Meijer WJJ]]
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[[Category: Phi-29 replication]]
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[[Category: Munoz-Espin D]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:23:03 2008''
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[[Category: Salas M]]
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[[Category: Villar L]]

Current revision

Solution structure of the functional domain of phi29 replication organizer p16.7c

PDB ID 1zae

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