Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine

Chang Hwa Jo, Junsoo Kim, Ah reum Han, Sam Yong Park, Kwang Yeon Hwang, Ki Hyun Nam

Research output: Contribution to journalArticle

4 Citations (Scopus)


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 languageEnglish
JournalFEBS Letters
Publication statusAccepted/In press - 2016



  • C-shape clamp
  • cis-cleavage mode
  • Tyrosine site-specific recombinase
  • Xer recombinase
  • XerA

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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