1hei: Difference between revisions
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[[Image:1hei.gif|left|200px]] | [[Image:1hei.gif|left|200px]] | ||
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN''' | {{Structure | ||
|PDB= 1hei |SIZE=350|CAPTION= <scene name='initialview01'>1hei</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HEI is a [ | 1HEI is a [[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)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEI OCA]. | ||
==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:// | 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] | ||
[[Category: Hepatitis c virus genotype 1a (isolate 1)]] | [[Category: Hepatitis c virus genotype 1a (isolate 1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna]] | [[Category: rna]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:06 2008'' | ||
Revision as of 09:36, 20 March 2008
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| 1hei, resolution 2.1Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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