Summary information and primary citation
- PDB-id
-
1nb7;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transferase-RNA
- Method
- X-ray (2.9 Å)
- Summary
- Hc-j4 RNA polymerase complexed with short RNA template
strand
- Reference
-
O'Farrell D, Trowbridge R, Rowlands D, Jager J (2003):
"Substrate
complexes of hepatitis C virus RNA polymerase (HC-J4):
structural evidence for nucleotide import and de-novo
initiation." J.Mol.Biol.,
326, 1025-1035. doi: 10.1016/S0022-2836(02)01439-0.
- Abstract
- Several crystal structures of the hepatitis C virus
NS5B protein (genotype-1b, strain J4) complexed with metal
ions, single-stranded RNA or nucleoside-triphosphates have
been determined. These complexes illustrate how conserved
amino acid side-chains, together with essential structural
features within the active site, control nucleotide binding
and likely mediate de-novo initiation. The incoming
nucleotide interacts with several basic residues from an
extension on the NS5B fingers domain, a beta-hairpin from
the NS5B thumb domain and the C-terminal arm. The modular,
bi-partite fingers domain carries a long binding groove
which guides the template towards the catalytic site. The
apo-polymerase structure provides unprecedented insights
into potential non-nucleoside inhibitor binding sites
located between palm and thumb near motif E, which is
unique to RNA polymerases and reverse transcriptases.