Cited by 138Bacterial Genetics and BiotechnologyDNA Repair MechanismsEnzyme Structure and Function

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The Mu transpososome structure sheds light on DDE recombinase evolution

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Montaño, Sherwin P., Pigli, Ying Z., Rice, Phoebe A.·2012·Nature

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Abstract

Studies of bacteriophage Mu transposition paved the way for understanding retroviral integration and V(D)J recombination as well as many other DNA transposition reactions. Here we report the structure of the Mu transpososome--Mu transposase (MuA) in complex with bacteriophage DNA ends and target DNA--determined from data that extend anisotropically to 5.2 Å, 5.2 Å and 3.7 Å resolution, in conjunction with previously determined structures of individual domains. The highly intertwined structure illustrates why chemical activity depends on formation of the synaptic complex, and reveals that individual domains have different roles when bound to different sites. The structure also provides explanations for the increased stability of the final product complex and for its preferential recognition by the ATP-dependent unfoldase ClpX. Although MuA and many other recombinases share a structurally conserved 'DDE' catalytic domain, comparisons among the limited set of available complex structures indicate that some conserved features, such as catalysis in trans and target DNA bending, arose through convergent evolution because they are important for function.

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Sheldrick, G. M. (2007) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 88,113
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Features and development of Coot
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Methods in Enzymology , Vol
Colowick, S. P., Joshi, M. D., Jagannathan, & KAPLAN, N. O. (1966) · Cited by 26,137
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
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Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
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Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
PHENIX: a comprehensive Python-based system for macromolecular structure solution
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Strong, M., Sawaya, M. R., Wang, S., Phillips, M. L., Cascio, D., & Eisenberg, D. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602606103 · Cited by 704

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Authors: Montaño, S. P., Pigli, Y. Z., & Rice, P. A.
Affiliations: University of Chicago (US)
Corresponding author: Rice, Phoebe A.
ORCID: Rice, Phoebe A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2012-11
Volume: 491
Issue: 7424
Pages: 413-417
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature11602
PMC: PMC3536463
OpenAlex: W2034741116
Cited by: 137
References: 65
Citations by year: 2026: 4 · 2025: 4 · 2024: 4 · 2023: 12 · 2022: 7 · 2021: 13 · 2020: 9 · 2019: 9 · 2018: 6 · 2017: 12 · 2016: 8 · 2015: 24 · 2014: 13 · 2013: 11 · 2012: 1
FWCI: 9.40
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: National Institute of General Medical Sciences (GM086826, R01GM086826)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: bacteriophage Mu, transpososome, DNA transposition, synaptic complex, transposon ends, target DNA, convergent evolution, protein-DNA complex structure
MeSH terms: DNA, Viral, Models, Molecular, Bacteriophage mu, Protein Binding, Protein Structure, Tertiary, Evolution, Molecular, Transposases, Recombinases

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The Mu transpososome structure sheds light on DDE recombinase evolution

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