5hxy
From Proteopedia
Crystal structure of XerA recombinase
Structural highlights
FunctionQ9HIM5_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 PubMedSite-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 AlsoReferences
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