Abstract
PriA, a DEXH-type DNA helicase, binds specifically to the 3' end of DNA through its N-terminal domain, and is a candidate sensor protein that recognizes arrested DNA replication forks in bacteria. We crystallized an N-terminal fragment of PriA in the absence and the presence of oligonucleotides to elucidate the structural basis for the specific recognition of the 3' terminus of DNA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Binding Sites
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Crystallization
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Crystallography, X-Ray
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DNA Helicases / chemistry*
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DNA Helicases / genetics
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DNA Helicases / metabolism
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins
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Oligodeoxyribonucleotides / chemistry
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Oligodeoxyribonucleotides / metabolism
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Escherichia coli Proteins
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Oligodeoxyribonucleotides
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Peptide Fragments
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Recombinant Proteins
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Adenosine Triphosphatases
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priA protein, E coli
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DNA Helicases