title: Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.
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.
authors.affiliation: Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
authors.forename: Chang Hwa
authors.initials: CH
authors.lastname: Jo
authors.affiliation: Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
authors.forename: Junsoo
authors.initials: J
authors.lastname: Kim
authors.affiliation: Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
authors.forename: Ah-reum
authors.initials: AR
authors.lastname: Han
authors.affiliation: Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Kanagawa, Japan.
authors.forename: Sam Yong
authors.initials: SY
authors.lastname: Park
authors.affiliation: Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
authors.forename: Kwang Yeon
authors.initials: KY
authors.lastname: Hwang
authors.affiliation: Pohang Accelerator Laboratory, Pohang University of Science and Technology, Kyungbuk, Korea.
authors.forename: Ki Hyun
authors.initials: KH
authors.lastname: Nam
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D019766:Genes, Archaeal; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D045522:Recombinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D013822:Thermoplasma / Q000201:enzymology* / Q000235:genetics; D014443:Tyrosine / Q000737:chemistry
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D045522:Recombinases; D014443:Tyrosine
keywords: C-shape clamp; Xer recombinase; XerA; cis-cleavage mode; tyrosine site-specific recombinase