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

3 Citations (Scopus)

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 languageEnglish
JournalFEBS Letters
DOIs
Publication statusAccepted/In press - 2016

Fingerprint

Thermoplasma
Recombinases
Clamping devices
Tyrosine
Conformations
Crystal structure
Nucleophiles
Genetic Recombination
Catalytic Domain
Monomers
DNA
Substrates

Keywords

  • 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

Cite this

Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine. / Jo, Chang Hwa; Kim, Junsoo; Han, Ah reum; Park, Sam Yong; Hwang, Kwang Yeon; Nam, Ki Hyun.

In: FEBS Letters, 2016.

Research output: Contribution to journalArticle

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AU - Park, Sam Yong

AU - Hwang, Kwang Yeon

AU - Nam, Ki Hyun

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