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PDBsum entry 3o8r
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Hydrolase/RNA
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PDB id
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3o8r
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References listed in PDB file
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Key reference
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Title
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Visualizing ATP-Dependent RNA translocation by the ns3 helicase from hcv.
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Authors
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T.C.Appleby,
R.Anderson,
O.Fedorova,
A.M.Pyle,
R.Wang,
X.Liu,
K.M.Brendza,
J.R.Somoza.
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Ref.
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J Mol Biol, 2011,
405,
1139-1153.
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PubMed id
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Abstract
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The structural mechanism by which nonstructural protein 3 (NS3) from the
hepatitis C virus (HCV) translocates along RNA is currently unknown. HCV NS3 is
an ATP-dependent motor protein essential for viral replication and a member of
the superfamily 2 helicases. Crystallographic analysis using a labeled RNA
oligonucleotide allowed us to unambiguously track the positional changes of RNA
bound to full-length HCV NS3 during two discrete steps of the ATP hydrolytic
cycle. The crystal structures of HCV NS3, NS3 bound to bromine-labeled RNA, and
a tertiary complex of NS3 bound to labeled RNA and a non-hydrolyzable ATP analog
provide a direct view of how large domain movements resulting from ATP binding
and hydrolysis allow the enzyme to translocate along the phosphodiester
backbone. While directional translocation of HCV NS3 by a single base pair per
ATP hydrolyzed is observed, the 3' end of the RNA does not shift register with
respect to a conserved tryptophan residue, supporting a
"spring-loading" mechanism that leads to larger steps by the enzyme as
it moves along a nucleic acid substrate.
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