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PDBsum entry 2p6u

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DNA binding protein PDB id
2p6u
Contents
Protein chain
671 a.a.
Ligands
PO4 ×10

References listed in PDB file
Key reference
Title Structural basis for DNA duplex separation by a superfamily-2 helicase.
Authors K.Büttner, S.Nehring, K.P.Hopfner.
Ref. Nat Struct Biol, 2007, 14, 647-652. [DOI no: 10.1038/nsmb1246]
PubMed id 17558417
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.
Figure 1.
(a) Schematic of the five domains of Hel308. Domain boundaries are indicated on top, sequence motifs beneath. Roman numerals, SF2 helicase motifs; , -hairpin loop; R, ratchet helix; RAR, Arg-Ala-Arg motif. (b) Hel308 (ribbon, colored as in a) in complex with the 15-base-pair DNA duplex and 10-base single-stranded 3' tail (beige sticks). (c) Schematic showing key interactions (dashed lines) of Hel308 with the partially unwound DNA substrate.
Figure 4.
Shown are products of proteolysis digestion of archaeal Hel308 by indicated amounts of proteinase K in the presence or absence of AMP-PNP and DNA.
The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 647-652) copyright 2007.
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