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1hei

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[[Image:1hei.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1hei| PDB=1hei | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hei OCA], [http://www.ebi.ac.uk/pdbsum/1hei PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hei RCSB]</span>
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'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/9187654 9187654]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9187654 9187654]
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[[Category: Hepatitis c virus genotype 1a (isolate 1)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Weber, P.]]
[[Category: Weber, P.]]
[[Category: Yao, N.]]
[[Category: Yao, N.]]
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[[Category: atpase]]
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[[Category: Atpase]]
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[[Category: hcv]]
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[[Category: Hcv]]
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[[Category: helicase]]
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[[Category: Helicase]]
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[[Category: hepatitis]]
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[[Category: Hepatitis]]
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[[Category: ntpase]]
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[[Category: Ntpase]]
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[[Category: rna]]
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[[Category: Rna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:46:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:03:30 2008''
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Revision as of 15:46, 2 May 2008

Image:1hei.gif

Template:STRUCTURE 1hei

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). 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 Page seeded by OCA on Fri May 2 18:46:06 2008

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