1HEI

STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN

Summary for 1HEI

• Entry DOI: 10.2210/pdb1hei/pdb
• Descriptor: HCV HELICASE, CALCIUM ION (3 entities in total)
• Functional Keywords: helicase, rna, hepatitis, hcv, atpase, ntpase
• Biological source: Hepatitis C virus (isolate 1)
• Cellular location: Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P27958
• Total number of polymer chains: 2
• Total formula weight: 96795.98

Authors

Yao, N.,Weber, P. (deposition date: 1997-03-31, release date: 1998-10-07, Last modification date: 2024-02-07)

Primary citation

Yao, N.,Hesson, T.,Cable, M.,Hong, Z.,Kwong, A.D.,Le, H.V.,Weber, P.C.
Structure of the hepatitis C virus RNA helicase domain.
Nat.Struct.Biol., 4:463-467, 1997

PubMed Abstract: 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.

PubMed: 9187654
DOI: 10.1038/nsb0697-463

Experimental method

X-RAY DIFFRACTION (2.1 Å)