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

Authors
Jo, Chang HwaKim, JunsooHan, Ah-reumPark, Sam YongHwang, Kwang YeonNam, Ki Hyun
Issue Date
3월-2016
Publisher
WILEY
Keywords
cis-cleavage mode; C-shape clamp; tyrosine site-specific recombinase; Xer recombinase; XerA
Citation
FEBS LETTERS, v.590, no.6, pp.848 - 856
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
590
Number
6
Start Page
848
End Page
856
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/89266
DOI
10.1002/1873-3468.12109
ISSN
0014-5793
Abstract
Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 angstrom 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 similar to 48 degrees and a distance of 57 angstrom 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.
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