2v9p: Difference between revisions

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[[Image:2v9p.png|left|200px]]


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==Crystal structure of papillomavirus E1 hexameric helicase DNA-free form==
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<StructureSection load='2v9p' size='340' side='right'caption='[[2v9p]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2v9p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Deltapapillomavirus_4 Deltapapillomavirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V9P 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]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_2v9p|  PDB=2v9p  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9p OCA], [https://pdbe.org/2v9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v9p RCSB], [https://www.ebi.ac.uk/pdbsum/2v9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v9p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VE1_BPV1 VE1_BPV1] 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/v9/2v9p_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=2v9p ConSurf].
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== Publication Abstract from PubMed ==
Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first time observed in the absence of nucleotide cofactors and DNA. Surprisingly, the ATP-binding sites adopt specific conformations linked to positional changes in the DNA-binding hairpins, which follow a wave-like trajectory, as observed previously in the E1/DNA/ADP complex. The protein's assembly thus maintains such an asymmetric state in the absence of DNA and nucleotide cofactors, allowing consideration of the E1 helicase action as the propagation of a conformational wave around the protein ring. The data imply that the wave's propagation within the AAA+ domains is not necessarily coupled with a strictly sequential hydrolysis of ATP. Since a single ATP hydrolysis event would affect the whole hexamer, such events may simply serve to rectify the direction of the wave's motion.


===CRYSTAL STRUCTURE OF PAPILLOMAVIRUS E1 HEXAMERIC HELICASE DNA-FREE FORM===
Papillomavirus E1 helicase assembly maintains an asymmetric state in the absence of DNA and nucleotide cofactors.,Sanders CM, Kovalevskiy OV, Sizov D, Lebedev AA, Isupov MN, Antson AA Nucleic Acids Res. 2007;35(19):6451-7. Epub 2007 Sep 19. PMID:17881379<ref>PMID:17881379</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2v9p" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17881379}}, adds the Publication Abstract to the page
*[[Helicase 3D structures|Helicase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17881379 is the PubMed ID number.
*[[Replication protein E1|Replication protein E1]]
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== References ==
{{ABSTRACT_PUBMED_17881379}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
2V9P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_papillomavirus_type_1 Bovine papillomavirus type 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9P OCA].
[[Category: Deltapapillomavirus 4]]
 
[[Category: Large Structures]]
==Reference==
[[Category: Antson AA]]
Papillomavirus E1 helicase assembly maintains an asymmetric state in the absence of DNA and nucleotide cofactors., Sanders CM, Kovalevskiy OV, Sizov D, Lebedev AA, Isupov MN, Antson AA, Nucleic Acids Res. 2007;35(19):6451-7. Epub 2007 Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17881379 17881379]
[[Category: Isupov MN]]
[[Category: Bovine papillomavirus type 1]]
[[Category: Kovalevskiy OV]]
[[Category: Single protein]]
[[Category: Lebedev AA]]
[[Category: Antson, A A.]]
[[Category: Sanders CM]]
[[Category: Isupov, M N.]]
[[Category: Sizov D]]
[[Category: Kovalevskiy, O V.]]
[[Category: Lebedev, A A.]]
[[Category: Sanders, C M.]]
[[Category: Sizov, D.]]
[[Category: Aaa+ molecular motor]]
[[Category: Atp-binding]]
[[Category: Atpase]]
[[Category: Dna replication]]
[[Category: Dna translocation]]
[[Category: Dna-binding]]
[[Category: Early protein]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Nucleotide-binding]]
[[Category: Nucleus]]
[[Category: Replication]]
 
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