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3O8C

Visualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCV

Summary for 3O8C
Entry DOI10.2210/pdb3o8c/pdb
Related1CU1 3O8B 3O8D 3O8R
DescriptorHCV NS3 protease/helicase, RNA (5'-R(P*UP*(5BU)P*UP*UP*UP*U)-3'), ZINC ION, ... (5 entities in total)
Functional Keywordshelicase, ntpase, hcv, rna, translocation, protease/ntpase/helicase, hydrolase-rna complex, hydrolase/rna
Biological sourceHepatitis C virus subtype 1b
More
Total number of polymer chains3
Total formula weight143932.66
Authors
Appleby, T.C.,Somoza, J.R. (deposition date: 2010-08-02, release date: 2011-01-05, Last modification date: 2023-09-06)
Primary citationAppleby, T.C.,Anderson, R.,Fedorova, O.,Pyle, A.M.,Wang, R.,Liu, X.,Brendza, K.M.,Somoza, J.R.
Visualizing ATP-Dependent RNA Translocation by the NS3 Helicase from HCV.
J.Mol.Biol., 405:1139-1153, 2011
Cited by
PubMed Abstract: 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.
PubMed: 21145896
DOI: 10.1016/j.jmb.2010.11.034
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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