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New page: left|200px<br /><applet load="1tue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tue, resolution 2.10Å" /> '''The X-ray Structure ...
 
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[[Image:1tue.gif|left|200px]]<br /><applet load="1tue" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tue, resolution 2.10&Aring;" />
'''The X-ray Structure of the Papillomavirus Helicase in Complex with its Molecular Matchmaker E2'''<br />


==Overview==
==The X-ray Structure of the Papillomavirus Helicase in Complex with its Molecular Matchmaker E2==
DNA replication of the papillomaviruses is specified by cooperative, binding of two proteins to the ori site: the enhancer E2 and the viral, initiator E1, a distant member of the AAA+ family of proteins. Formation, of this prereplication complex is an essential step toward the, construction of a functional, multimeric E1 helicase and DNA melting. To, understand how E2 interacts with E1 to regulate this process, we have, solved the X-ray structure of a complex containing the HPV18 E2 activation, domain bound to the helicase domain of E1. Modeling the monomers of E1 to, a hexameric helicase shows that E2 blocks hexamerization of E1 by, shielding a region of the E1 oligomerization surface and stabilizing a, conformation of E1 that is incompatible with ATP binding. Further, biochemical experiments and structural analysis show that ATP is an, allosteric effector of the dissociation of E2 from E1. Our data provide, the first molecular insights into how a protein can regulate the assembly, of an oligomeric AAA+ complex and explain at a structural level why E2, after playing a matchmaker role by guiding E1 to the DNA, must dissociate, for subsequent steps of initiation to occur. Building on previously, proposed ideas, we discuss how our data advance current models for the, conversion of E1 in the prereplication complex to a hexameric helicase, assembly.
<StructureSection load='1tue' size='340' side='right'caption='[[1tue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tue]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_papillomavirus_type_18 Human papillomavirus type 18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=1tue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tue OCA], [https://pdbe.org/1tue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tue RCSB], [https://www.ebi.ac.uk/pdbsum/1tue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tue ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VE1_HPV18 VE1_HPV18] ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tu/1tue_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1tue ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TUE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_63 Human papillomavirus type 63]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TUE OCA].
*[[Helicase 3D structures|Helicase 3D structures]]
 
*[[Regulatory protein E2|Regulatory protein E2]]
==Reference==
*[[Replication protein E1|Replication protein E1]]
The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2., Abbate EA, Berger JM, Botchan MR, Genes Dev. 2004 Aug 15;18(16):1981-96. Epub 2004 Aug 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15289463 15289463]
__TOC__
[[Category: Human papillomavirus type 63]]
</StructureSection>
[[Category: Protein complex]]
[[Category: Human papillomavirus type 18]]
[[Category: Abbate, E.A.]]
[[Category: Large Structures]]
[[Category: Berger, J.M.]]
[[Category: Abbate EA]]
[[Category: Botchan, M.R.]]
[[Category: Berger JM]]
[[Category: aaa+ protein]]
[[Category: Botchan MR]]
[[Category: e1e2 complex]]
[[Category: helicase]]
[[Category: human papillomavirus]]
[[Category: replication]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:35:59 2007''

Latest revision as of 08:42, 14 February 2024

The X-ray Structure of the Papillomavirus Helicase in Complex with its Molecular Matchmaker E2

1tue, resolution 2.10Å

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