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1hei
From Proteopedia
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|PDB= 1hei |SIZE=350|CAPTION= <scene name='initialview01'>1hei</scene>, resolution 2.1Å | |PDB= 1hei |SIZE=350|CAPTION= <scene name='initialview01'>1hei</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Weber, P.]] | [[Category: Weber, P.]] | ||
[[Category: Yao, N.]] | [[Category: Yao, N.]] | ||
| - | [[Category: CA]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: hcv]] | [[Category: hcv]] | ||
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[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:03:30 2008'' |
Revision as of 18:03, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:03:30 2008
Categories: Hepatitis c virus genotype 1a (isolate 1) | Single protein | Weber, P. | Yao, N. | Atpase | Hcv | Helicase | Hepatitis | Ntpase | Rna
