Cited by 310DNA Repair MechanismsEnzyme Structure and FunctionProtein Structure and Dynamics

Crystal structure of a Rad51 filament

Conway, Adam B, Lynch, Thomas W, Zhang, Ying, Fortin, Gary S, Fung, Cindy W, Symington, Lorraine S, Rice, Phoebe A·2004·Nature Structural & Molecular Biology

Abstract

Rad51, the major eukaryotic homologous recombinase, is important for the repair of DNA damage and the maintenance of genomic diversity and stability. The active form of this DNA-dependent ATPase is a helical filament within which the search for homology and strand exchange occurs. Here we present the crystal structure of a Saccharomyces cerevisiae Rad51 filament formed by a gain-of-function mutant. This filament has a longer pitch than that seen in crystals of Rad51's prokaryotic homolog RecA, and places the ATPase site directly at a new interface between protomers. Although the filament exhibits approximate six-fold symmetry, alternate protein-protein interfaces are slightly different, implying that the functional unit of Rad51 within the filament may be a dimer. Additionally, we show that mutation of His352, which lies at this new interface, markedly disrupts DNA binding.

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Crossref · 10.1038/nsmb795

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  • The model of the trimeric Rad55-Rad57-Rad51 complex, in combination with the known Rad51 filament structure, suggests that Rad55-Rad57 binds at the 5' end of the Rad51 filament where it could promote growth of the Rad51 filament in a directional manner.

    “We generated a model of the trimeric Rad55–Rad57–Rad51 complex, which in combination with the known Rad51 filament structure (37), suggests that Rad55–Rad57 binds at the 5’ end of the Rad51 filament where it could promote growth of the Rad51 filament in a directional manner (Fig. 5B and fig. S18).”

    From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [37]

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Authors
Conway, A. B., Lynch, T. W., Zhang, Y., Fortin, G. S., Fung, C. W., Symington, L. S., & Rice, P. A.
Affiliations
  • University of Chicago (US)
  • Fox Chase Cancer Center (US)
  • Columbia University (US)
Corresponding author
Rice, Phoebe A
Venue
Nature Structural & Molecular Biology
Published
2004-07-04
Volume
11
Issue
8
Pages
791-796
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2066616729
Cited by
310
References
40
Citations by year
2026: 6 · 2025: 17 · 2024: 7 · 2023: 10 · 2022: 5 · 2021: 11 · 2020: 9 · 2019: 12 · 2018: 15 · 2017: 8 · 2016: 25 · 2015: 7 · 2014: 16 · 2013: 14 · 2012: 16
FWCI
7.95
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Structural & Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Cancer Institute (T32CA09594, T32 CA 09503, T32CA009503, T32CA009594)
  • National Institute of General Medical Sciences (R01GM058827, R01GM054099, GM 54099, T32GM008720, GM058827)
  • National Center for Research Resources (RR07 707)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
RAD51, homologous recombination, DNA-dependent ATPase, helical filaments, RecA, DNA strand exchange, DNA repair, genome stability, protein-protein interfaces, ATPase site, hexagonal symmetry, dimers, DNA binding, Saccharomyces cerevisiae
MeSH terms
Adenosine Triphosphatases, Adenosine Triphosphate, DNA, DNA Damage, DNA-Binding Proteins, Histidine, Hydrogen-Ion Concentration, Hydrolysis, Models, Molecular, Mutation, Phosphorylation, Protein Binding, Protein Conformation, Rec A Recombinases, Saccharomyces cerevisiae, Time Factors, Tyrosine, Crystallography, X-Ray, Saccharomyces cerevisiae Proteins, Rad51 Recombinase

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