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PDBsum entry 4idh
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Viral protein
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PDB id
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4idh
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References listed in PDB file
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Key reference
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Title
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Structures of the phage sf6 large terminase provide new insights into DNA translocation and cleavage.
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Authors
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H.Zhao,
T.E.Christensen,
Y.N.Kamau,
L.Tang.
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Ref.
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Proc Natl Acad Sci U S A, 2013,
110,
8075-8080.
[DOI no: ]
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PubMed id
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Abstract
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Many DNA viruses use powerful molecular motors to cleave concatemeric viral DNA
into genome-length units and package them into preformed procapsid powered by
ATP hydrolysis. Here we report the structures of the DNA-packaging motor gp2 of
bacteriophage Sf6, which reveal a unique clade of RecA-like ATPase domain and an
RNase H-like nuclease domain tethered by a regulatory linker domain, exhibiting
a strikingly distinct domain arrangement. The gp2 structures complexed with
nucleotides reveal, at the atomic detail, the catalytic center embraced by the
ATPase domain and the linker domain. The gp2 nuclease activity is modulated by
the ATPase domain and is stimulated by ATP. An extended DNA-binding surface is
formed by the linker domain and the nuclease domain. These results suggest a
unique mechanism for translation of chemical reaction into physical motion of
DNA and provide insights into coordination of DNA translocation and cleavage in
a viral DNA-packaging motor, which may be achieved via linker-domain-mediated
interdomain communication driven by ATP hydrolysis.
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