title: Structure of the hypothetical protein Ton1535 from Thermococcus onnurineus NA1 reveals unique structural properties by a left-handed helical turn in normal α-solenoid protein.
abstract: The crystal structure of Ton1535, a hypothetical protein from Thermococcus onnurineus NA1, was determined at 2.3 Å resolution. With two antiparallel α-helices in a helix-turn-helix motif as a repeating unit, Ton1535 consists of right-handed coiled N- and C-terminal regions that are stacked together using helix bundles containing a left-handed helical turn. One left-handed helical turn in the right-handed coiled structure produces two unique structural properties. One is the presence of separated concave grooves rather than one continuous concave groove, and the other is the contribution of α-helices on the convex surfaces of the N-terminal region to the extended surface of the concave groove of the C-terminal region and vice versa.
authors.affiliation: Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Republic of Korea.
authors.forename: Jae-Hee
authors.initials: JH
authors.lastname: Jeong
authors.forename: Yi-Seul
authors.initials: YS
authors.lastname: Kim
authors.forename: Catleya
authors.initials: C
authors.lastname: Rojvirija
authors.forename: Hyung Jin
authors.initials: HJ
authors.lastname: Cha
authors.forename: Yeon-Gil
authors.initials: YG
authors.lastname: Kim
authors.forename: Sung Chul
authors.initials: SC
authors.lastname: Ha
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D019712:Thermococcus
chemical_list: D019843:Archaeal Proteins
keywords: Thermococcus onnurineus NA1; Ton1535; hypothetical protein; left-handed helical turn; right-handed coiled coil; solenoid protein