1NB4

HC-J4 RNA polymerase apo-form

Summary for 1NB4

• Entry DOI: 10.2210/pdb1nb4/pdb
• Related: 1NB7 1nb6
• Descriptor: polyprotein (2 entities in total)
• Functional Keywords: hepatitis c virus, replication, rna polymerase, de-novo priming, function analysis, hcv, ns5b, rdrp, transferase
• Biological source: Hepatitis C virus
• Total number of polymer chains: 2
• Total formula weight: 126913.48

Authors

Jaeger, J.,O'Farrell, D.J.,Trowbridge, R.,Rowlands, D.J. (deposition date: 2002-12-02, release date: 2003-03-25, Last modification date: 2023-08-16)

Primary citation

O'Farrell, D.,Trowbridge, R.,Rowlands, D.,Jager, J.
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, 2003

PubMed 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.

PubMed: 12589751
DOI: 10.1016/S0022-2836(02)01439-0

Experimental method

X-RAY DIFFRACTION (2 Å)