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PDBsum entry 3e1s
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References listed in PDB file
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Key reference
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Title
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Dna binding to recd: role of the 1b domain in sf1b helicase activity.
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Authors
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K.Saikrishnan,
S.P.Griffiths,
N.Cook,
R.Court,
D.B.Wigley.
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Ref.
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Embo J, 2008,
27,
2222-2229.
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PubMed id
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Abstract
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The molecular mechanism of superfamily 1Balpha helicases remains unclear. We
present here the crystal structure of the RecD2 helicase from Deinococcus
radiodurans at 2.2-A resolution. The structure reveals the folds of the 1B and
2B domains of RecD that were poorly ordered in the structure of the Escherichia
coli RecBCD enzyme complex reported previously. The 2B domain adopts an SH3 fold
which, although common in eukaryotes, is extremely rare in bacterial systems. In
addition, the D. radiodurans RecD2 structure has aided us in deciphering lower
resolution (3.6 A) electron density maps for the E. coli RecBCD enzyme in
complex with a long DNA substrate that interacts with the RecD subunit. Taken
together, these structures indicated an important role for the 1B domain of
RecD, a beta-hairpin that extends from the surface of the 1A domain and
interacts with the DNA substrate. On the basis of these structural data, we
designed a mutant RecD2 helicase that lacks this pin. The 'pin-less' mutant
protein is a fully active ssDNA-dependent ATPase but totally lacks helicase
activity.
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