1hei: Difference between revisions
New page: left|200px<br /><applet load="1hei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hei, resolution 2.1Å" /> '''STRUCTURE OF THE HEPA... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1hei.gif|left|200px]]<br /><applet load="1hei" size=" | [[Image:1hei.gif|left|200px]]<br /><applet load="1hei" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hei, resolution 2.1Å" /> | caption="1hei, resolution 2.1Å" /> | ||
'''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''<br /> | '''STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Helicases are nucleotide triphosphate (NTP)-dependent enzymes responsible | 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== | ||
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:// | 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== | ||
| Line 23: | Line 23: | ||
[[Category: rna]] | [[Category: rna]] | ||
''Page seeded by [http:// | ''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
|
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 CA 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
Page seeded by OCA on Thu Feb 21 13:00:27 2008
