title: Resonance assignments of a putative PilT N-terminus domain protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2.
abstract: PilT N-terminus (PIN) domains exist broadly in all three kingdoms of life, but the functions are not clear for most of them. Archaea species often encode multiple PIN domain-containing proteins, and the signaling and stress response roles have been proposed for these proteins. Some PIN domain proteins possess nuclease activities, which were proposed to be important in toxin-antitoxin stress response, nonsense-mediated mRNA decay, or RNA interference. SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2 is a putative PIN domain protein with low homology to other known PIN domain proteins. Here we report the NMR resonance assignments of SSO1118 for further structural determination and functional studies. The secondary structures predicted from the assigned chemical shifts consist with those of archaeal PIN domain proteins.
authors.affiliation: Department of Biological Science and Engineering, School of Chemical and Biological Engineering, University of Science and Technology Beijing, 30 Xueyuan Road, Beijing, 100083, China. jsxuan@sas.ustb.edu.cn
authors.forename: Jinsong
authors.initials: J
authors.lastname: Xuan
authors.forename: Xiaxia
authors.initials: X
authors.lastname: Song
authors.forename: Jinfeng
authors.initials: J
authors.lastname: Wang
authors.forename: Yingang
authors.initials: Y
authors.lastname: Feng
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D048229:Sulfolobus solfataricus / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins