5HXY

Crystal structure of XerA recombinase

Summary for 5HXY

• Entry DOI: 10.2210/pdb5hxy/pdb
• Descriptor: Tyrosine recombinase XerA, PHOSPHATE ION (3 entities in total)
• Functional Keywords: recombinase, xera, recombination
• Biological source: Thermoplasma acidophilum DSM 1728
• Total number of polymer chains: 6
• Total formula weight: 223703.03

Authors

Hwang, K.Y.,Nam, K.H. (deposition date: 2016-01-31, release date: 2017-02-01, Last modification date: 2024-11-20)

Primary citation

Jo, C.H.,Kim, J.,Han, A.R.,Park, S.Y.,Hwang, K.Y.,Nam, K.H.
Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine
FEBS Lett., 590:848-856, 2016

PubMed 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.

PubMed: 26919387
DOI: 10.1002/1873-3468.12109

Experimental method

X-RAY DIFFRACTION (2.5 Å)