Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.
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.
Meier
Sebastian
S
Division of Structural Biology, Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Häussinger
Daniel
D
Pokidysheva
Elena
E
Bächinger
Hans Peter
HP
Grzesiek
Stephan
S
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
D004220:Disulfides; D003094:Collagen; D005978:Glutathione; D003545:Cysteine; D019803:Glutathione Disulfide