1hei

From Proteopedia

Revision as of 14:25, 20 November 2007

STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN

Overview

Helicases are nucleotide triphosphate (NTP)-dependent enzymes responsible, for unwinding duplex DNA and RNA during genomic replication. The 2.1 A, resolution structure of the HCV helicase from the positive-stranded RNA, hepatitis C virus reveals a molecule with distinct NTPase and RNA binding, domains. The structure supports a mechanism of helicase activity involving, initial recognition of the requisite 3' single-stranded region on the, nucleic acid substrate by a conserved arginine-rich sequence on the RNA, binding domain. Comparison of crystallographically independent molecules, shows that rotation of the RNA binding domain involves conformational, changes within a conserved TATPP sequence and untwisting of an extended, antiparallel beta-sheet. Location of the TATPP sequence at the end of an, NTPase domain beta-strand structurally homologous to the 'switch region', of many NTP-dependent enzymes offers the possibility that domain rotation, is coupled to NTP hydrolysis in the helicase catalytic cycle.

About this Structure

1HEI is a Single protein structure of sequence from Hepatitis c virus genotype 1a (isolate 1) with CA as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the hepatitis C virus RNA helicase domain., Yao N, Hesson T, Cable M, Hong Z, Kwong AD, Le HV, Weber PC, Nat Struct Biol. 1997 Jun;4(6):463-7. PMID:9187654

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