title: Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.
abstract: A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled.
authors.affiliation: Division of Structural Biology, Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Meier
authors.forename: Daniel
authors.initials: D
authors.lastname: Häussinger
authors.forename: Elena
authors.initials: E
authors.lastname: Pokidysheva
authors.forename: Hans Peter
authors.initials: HP
authors.lastname: Bächinger
authors.forename: Stephan
authors.initials: S
authors.lastname: Grzesiek
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry*; D003545:Cysteine / Q000032:analysis*; D004220:Disulfides / Q000032:analysis; D005978:Glutathione / Q000032:analysis; D019803:Glutathione Disulfide / Q000032:analysis; D006829:Hydra / Q000737:chemistry*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data
chemical_list: D004220:Disulfides; D003094:Collagen; D005978:Glutathione; D003545:Cysteine; D019803:Glutathione Disulfide