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1hei

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(New page: 200px<br /><applet load="1hei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hei, resolution 2.1&Aring;" /> '''STRUCTURE OF THE HEPA...)
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caption="1hei, resolution 2.1&Aring;" />
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''<br />
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1HEI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus_genotype_1a_(isolate_1) Hepatitis c virus genotype 1a (isolate 1)] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HEI OCA].
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1HEI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus_genotype_1a_(isolate_1) Hepatitis c virus genotype 1a (isolate 1)] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEI OCA].
==Reference==
==Reference==
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:32:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:27 2008''

Revision as of 11:00, 21 February 2008

Image:1hei.gif

1hei, resolution 2.1Å

Drag the structure with the mouse to rotate

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 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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