Crystal structure of a DExx box DNA helicase
Abstract
There are a wide variety of helicases that unwind helical DNA and RNA substrates. The twelve helicases that have been identified in Escherichia coli 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 A 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.
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Self-citation
- Authors
- Subramanya, H. S., Bird, L. E., Brannigan, J. A., & Wigley, D. B.
- Affiliations
- University of Oxford (GB)
- Venue
- Nature
- Published
- 1996-11
- Volume
- 384
- Issue
- 6607
- Pages
- 379-383
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2026133647
- Semantic Scholar
- a3754f9974c39e55f7ae1b8e9db633c4be7d328e
- Cited by
- 433
- References
- 29
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 2 · 2023: 5 · 2022: 2 · 2021: 8 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 6 · 2015: 5 · 2014: 12 · 2013: 19 · 2012: 12
- FWCI
- 32.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- DNA helicase, Bacillus stearothermophilus, crystal structure, ADP complex, ATP binding site, ATP hydrolysis, conformational change
- MeSH terms
- Adenosine Diphosphate, Amino Acid Sequence, Geobacillus stearothermophilus, DNA Helicases, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Rec A Recombinases, Conserved Sequence, Crystallography, X-Ray
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