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 |
|---|---|
| Journal | FEBS Letters |
| DOIs | |
| Publication status | Accepted/In press - 2016 |
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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 journal › Article
}
TY - JOUR
T1 - Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine
AU - Jo, Chang Hwa
AU - Kim, Junsoo
AU - Han, Ah reum
AU - Park, Sam Yong
AU - Hwang, Kwang Yeon
AU - Nam, Ki Hyun
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
KW - C-shape clamp
KW - cis-cleavage mode
KW - Tyrosine site-specific recombinase
KW - Xer recombinase
KW - XerA
UR - http://www.scopus.com/inward/record.url?scp=84960146242&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84960146242&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.12109
DO - 10.1002/1873-3468.12109
M3 - Article
C2 - 26919387
AN - SCOPUS:84960146242
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
ER -