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| [[Image:1hei.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1hei| PDB=1hei | SCENE= }} | | {{STRUCTURE_1hei| PDB=1hei | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9187654}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9187654 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9187654}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ntpase]] | | [[Category: Ntpase]] |
| [[Category: Rna]] | | [[Category: Rna]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:46:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:04:34 2008'' |
