7apd: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 7apd is ON HOLD
+==Bovine Papillomavirus E1 DNA helicase-replication fork complex==
+<StructureSection load='7apd' size='340' side='right'caption='[[7apd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7apd]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_papillomavirus Bovine papillomavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7APD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7APD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#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=7apd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7apd OCA], [https://pdbe.org/7apd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7apd RCSB], [https://www.ebi.ac.uk/pdbsum/7apd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7apd 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.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hexameric helicases are motor proteins that unwind double-stranded DNA (dsDNA) during DNA replication but how they are optimised for strand separation is unclear. Here we present the cryo-EM structure of the full-length E1 helicase from papillomavirus, revealing all arms of a bound DNA replication fork and their interactions with the helicase. The replication fork junction is located at the entrance to the helicase collar ring, that sits above the AAA + motor assembly. dsDNA is escorted to and the 5 single-stranded DNA (ssDNA) away from the unwinding point by the E1 dsDNA origin binding domains. The 3 ssDNA interacts with six spirally-arranged beta-hairpins and their cyclical top-to-bottom movement pulls the ssDNA through the helicase. Pulling of the RF against the collar ring separates the base-pairs, while modelling of the conformational cycle suggest an accompanying movement of the collar ring has an auxiliary role, helping to make efficient use of ATP in duplex unwinding.
-Authors: Javed, A., Major, B., Stead, J., Sanders, C.M., Orlova, E.V.
+Unwinding of a DNA replication fork by a hexameric viral helicase.,Javed A, Major B, Stead JA, Sanders CM, Orlova EV Nat Commun. 2021 Sep 20;12(1):5535. doi: 10.1038/s41467-021-25843-6. PMID:34545080<ref>PMID:34545080</ref>
-Description: Bovine Papillomavirus E1 DNA helicase-replication fork complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Major, B]]
+<div class="pdbe-citations 7apd" style="background-color:#fffaf0;"></div>
-[[Category: Sanders, C.M]]
-[[Category: Orlova, E.V]]
+==See Also==
-[[Category: Javed, A]]
+*[[Helicase 3D structures|Helicase 3D structures]]
-[[Category: Stead, J]]
+*[[Replication protein E1|Replication protein E1]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bovine papillomavirus]]
+[[Category: Large Structures]]
+[[Category: Javed A]]
+[[Category: Major B]]
+[[Category: Orlova EV]]
+[[Category: Sanders CM]]
+[[Category: Stead J]]