2P6U
Apo structure of the Hel308 superfamily 2 helicase
Summary for 2P6U
| Entry DOI | 10.2210/pdb2p6u/pdb |
| Descriptor | afuHEL308 HELICASE, PHOSPHATE ION (2 entities in total) |
| Functional Keywords | archaeal helicase, sf2 helicase, dna repair, dna binding protein |
| Biological source | Archaeoglobus fulgidus |
| Total number of polymer chains | 1 |
| Total formula weight | 80072.52 |
| Authors | Buettner, K.,Nehring, S.,Hopfner, K.P. (deposition date: 2007-03-19, release date: 2007-06-12, Last modification date: 2024-02-21) |
| Primary citation | Buttner, K.,Nehring, S.,Hopfner, K.P. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat.Struct.Mol.Biol., 14:647-652, 2007 Cited by PubMed Abstract: To reveal the mechanism of processive strand separation by superfamily-2 (SF2) 3'-->5' helicases, we determined apo and DNA-bound crystal structures of archaeal Hel308, a helicase that unwinds lagging strands and is related to human DNA polymerase theta. Our structure captures the duplex-unwinding reaction, shows that initial strand separation does not require ATP and identifies a prominent beta-hairpin loop as the unwinding element. Similar loops in hepatitis C virus NS3 helicase and RNA-decay factors support the idea that this duplex-unwinding mechanism is applicable to a broad subset of SF2 helicases. Comparison with ATP-bound SF2 enzymes suggests that ATP promotes processive unwinding of 1 base pair by ratchet-like transport of the 3' product strand. Our results provide a first structural framework for strand separation by processive SF2 3'-->5' helicases and reveal important mechanistic differences from SF1 helicases. PubMed: 17558417DOI: 10.1038/nsmb1246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.14 Å) |
Structure validation
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