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Determination of a high‐precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation
Author(s) -
Meier Sebastian,
Häussinger Daniel,
Pokidysheva Elena,
Bächinger Hans Peter,
Grzesiek Stephan
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.034
Subject(s) - cysteine , lernaean hydra , chemistry , characterization (materials science) , disulfide bond , stereochemistry , biochemistry , materials science , biology , nanotechnology , enzyme , microbiology and biotechnology
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.