Structural highlights
Function
[Q9HIM5_THEAC] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.[HAMAP-Rule:MF_02055]
Publication Abstract from PubMed
Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 A 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 degrees and a distance of 57 A 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.
Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.,Jo CH, Kim J, Han AR, Park SY, Hwang KY, Nam KH FEBS Lett. 2016 Mar;590(6):848-56. doi: 10.1002/1873-3468.12109. Epub 2016 Mar 4. PMID:26919387[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jo CH, Kim J, Han AR, Park SY, Hwang KY, Nam KH. Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine. FEBS Lett. 2016 Mar;590(6):848-56. doi: 10.1002/1873-3468.12109. Epub 2016 Mar 4. PMID:26919387 doi:http://dx.doi.org/10.1002/1873-3468.12109
