Study of the Atp-binding Site of Helicase Iv from Escherichia Coli.
From: Novartis Institutes for Biomedical Research, Oncology Department, CH-4002 Basel, Switzerland.
Biochemical and biophysical research communications
- Publish Date: Mar 2006
- ISSN: 0006-291X
- Volume: 341
- Issue: 3
- Pages: 828-36
- Medium: Print
- Language: English
- Citation (JAMA): Dubaele Sandy, Lourdel Claude, Chène Patrick, et al. Study of the Atp-binding Site of Helicase Iv from Escherichia Coli.. Biochem. Biophys. Res. Commun. Mar 2006;341:828-36
Abstract
Helicases contain conserved motifs involved in ATP/magnesium/nucleic acid binding and in the mechanisms coupling nucleotide hydrolysis to duplex unwinding. None of these motifs are located at the adenine-binding pocket of the protein. We show here that the superfamily I helicase, helicase IV from Escherichia coli, utilizes a conserved glutamine and conserved aromatic residue to interact with ATP. Other superfamily I helicases such as, UvrD/Rep/PcrA also possess these residues but in addition they interact with adenine via a conserved arginine, which is replaced by a serine in helicase IV. Mutation of this serine residue in helicase IV into histidine or methionine leads to proteins with unaffected ATPase and DNA-binding activities but with low helicase activity. This suggests that residues located at the adenine-binding pocket, in addition to be involved in ATP-binding, are important for efficient coupling between ATP hydrolysis and DNA unwinding.
Mesh Headings (Keywords): Adenine, Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Conserved Sequence, DNA Helicases, DNA, Bacterial, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Protein Structure, Tertiary, Sequence Alignment
Check for Full Text / PubMed Unique Identifier (PMID): 16442499
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