1SP7

Structure of the Cys-rich C-terminal domain of Hydra minicollagen

Summary for 1SP7

• Entry DOI: 10.2210/pdb1sp7/pdb
• NMR Information: BMRB: 6200
• Descriptor: mini-collagen (1 entity in total)
• Functional Keywords: cysteine-rich, proline-rich, disulfide bond, structural protein
• Total number of polymer chains: 1
• Total formula weight: 2595.20

Authors

Meier, S.,Haussinger, D.,Pokidysheva, E.,Bachinger, H.P.,Grzesiek, S. (deposition date: 2004-03-16, release date: 2004-05-18, Last modification date: 2024-10-30)

Primary citation

Meier, S.,Haussinger, D.,Pokidysheva, E.,Bachinger, H.P.,Grzesiek, S.
Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.
Febs Lett., 569:112-116, 2004

PubMed 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.

PubMed: 15225618
DOI: 10.1016/j.febslet.2004.05.034

Experimental method

SOLUTION NMR