7APD
Bovine Papillomavirus E1 DNA helicase-replication fork complex
Summary for 7APD
| Entry DOI | 10.2210/pdb7apd/pdb |
| EMDB information | 11852 |
| Descriptor | Replication protein E1, DNA (40-MER), DNA (36-MER), ... (4 entities in total) |
| Functional Keywords | dna, virus, helicase, replisome, dna replication., dna binding protein |
| Biological source | Bovine papillomavirus More |
| Total number of polymer chains | 10 |
| Total formula weight | 260702.07 |
| Authors | Javed, A.,Major, B.,Stead, J.,Sanders, C.M.,Orlova, E.V. (deposition date: 2020-10-16, release date: 2021-11-17, Last modification date: 2024-07-10) |
| Primary citation | Javed, A.,Major, B.,Stead, J.A.,Sanders, C.M.,Orlova, E.V. Unwinding of a DNA replication fork by a hexameric viral helicase. Nat Commun, 12:5535-5535, 2021 Cited by PubMed Abstract: 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 β-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. PubMed: 34545080DOI: 10.1038/s41467-021-25843-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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