Abstract
Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 Å crystal structure of XerA from the archaean Thermoplasma acidophilum. Crystallographic data reveal a uniquely open conformational state, resulting in a C-shaped clamp with an angle of ∼ 48° and a distance of 57 Å between the core-binding and the catalytic domains. The catalytic nucleophile, Tyr264, is positioned in cis-cleavage mode by XerA's C-term tail that interacts with the CAT domain of a neighboring monomer without DNA substrate. Structural comparisons of tyrosine recombinases elucidate the dynamics of Xer recombinase.
Original language | English |
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Pages (from-to) | 848-856 |
Number of pages | 9 |
Journal | FEBS Letters |
Volume | 590 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2016 Mar 1 |
Keywords
- C-shape clamp
- Xer recombinase
- XerA
- cis-cleavage mode
- tyrosine site-specific recombinase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology