The importance of the Q motif in the ATPase activity of a viral helicase
| Autor: | J.-P Gallivan, Michael J. McGarvey |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
NS3
DExD/H box helicase viruses ATPase medicine.medical_treatment Amino Acid Motifs Biophysics Viral Nonstructural Proteins Biology Q motif Biochemistry Encephalitis Viruses Tick-Borne Mice Adenosine Triphosphate Structural Biology ATP hydrolysis Escherichia coli Genetics medicine Animals Powassan virus Molecular Biology Sequence Deletion Adenosine Triphosphatases chemistry.chemical_classification Protease Hydrolysis DNA Helicases virus diseases Helicase DNA Cell Biology biochemical phenomena metabolism and nutrition biology.organism_classification RNA Helicase A Peptide Fragments Recombinant Proteins Amino acid DNA-Binding Proteins chemistry biology.protein Autoradiography RNA Viral |
| Zdroj: | FEBS Letters. 554:485-488 |
| ISSN: | 0014-5793 |
| Popis: | NS3 proteins of flaviviruses contain motifs which indicate that they possess protease and helicase activities. The helicases are members of the DExD/H box helicase superfamily and NS3 proteins from some flaviviruses have been shown to possess ATPase and helicase activities in vitro. The Q motif is a recently recognised cluster of nine amino acids common to most DExD/H box helicases which is proposed to regulate ATP binding and hydrolysis. In addition a conserved residue occurs 17 amino acids upstream of the Q motif (‘+17’). We have analysed full-length and truncated NS3 proteins from Powassan virus (a tick-borne flavivirus) to investigate the role that the Q motif plays in the hydrolysis of ATP by a viral helicase. The Q motif appears to be essential for the activity of Powassan virus NS3 ATPase, however NS3 deletion mutants that contain the Q motif but lack the ‘+17’ amino acid have ATPase activity albeit at a reduced level. |
| Databáze: | OpenAIRE |
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