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From the same journal

Crystal structure of a DExx box DNA helicase

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JournalNature
DatePublished - 28 Nov 1996
Issue number6607
Volume384
Number of pages5
Pages (from-to)379-383
Original languageEnglish

Abstract

THERE are a wide variety of helicases that unwind helical DNA(1) and RNA substrates(2). The twelve helicases that have been identified in Escherichia coli(1) play a role in almost all cellular processes involving nucleic acids, We have solved the crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermophilus, alone and in a complex with ADP, at 2.5 and 2.9 Angstrom resolution, respectively, The enzyme comprises two domains with a deep cleft running between them, The ATP-binding site, which is situated at the bottom of this cleft, is formed by motifs that are conserved across the superfamily of related helicases, Unexpected structural homology with the DNA recombination protein, RecA, suggests how ATP binding and hydrolysis may drive conformational changes of the enzyme during catalysis, and implies that there is a common mechanism for all helicases.

    Research areas

  • REPLICATION PROTEIN PRIA, COLI REP HELICASE, ESCHERICHIA-COLI, RNA HELICASE, BINDING, OVEREXPRESSION, DIMERIZATION, COMPONENT, MUTATIONS, PRIMOSOME

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