1NB7

HC-J4 RNA polymerase complexed with short RNA template strand

Summary for 1NB7

• Entry DOI: 10.2210/pdb1nb7/pdb
• Related: 1NB4 1NB6
• Descriptor: 5'-R(*UP*UP*UP*U)-3', polyprotein, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: hepatitis c virus, replication, rna polymerase, de-novo priming, function analysis, hcv, ns5b, rdrp, transferase-rna complex, transferase/rna
• Biological source: Hepatitis C virus
• Total number of polymer chains: 4
• Total formula weight: 129492.65

Authors

O'Farrell, D.J.,Trowbridge, R.,Rowlands, D.J.,Jaeger, J. (deposition date: 2002-12-02, release date: 2003-03-25, Last modification date: 2024-02-14)

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 (2.9 Å)