1SOP

C-terminal cystine-rich domain of Minicollagen-I from Hydra

Summary for 1SOP

• Entry DOI: 10.2210/pdb1sop/pdb
• Descriptor: mini-collagen (1 entity in total)
• Functional Keywords: collagen oxidative refolding, structural protein
• Total number of polymer chains: 1
• Total formula weight: 2619.24

Authors

Milbradt, A.G.,Moroder, L.,Renner, C. (deposition date: 2004-03-15, release date: 2004-04-27, Last modification date: 2022-03-02)

Primary citation

Pokidysheva, E.,Milbradt, A.G.,Meier, S.,Renner, C.,Haussinger, D.,Bachinger, H.P.,Moroder, L.,Grzesiek, S.,Holstein, T.W.,Ozbek, S.,Engel, J.
The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall.
J.Biol.Chem., 279:30395-30401, 2004

PubMed Abstract: The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by 1H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.

PubMed: 15123641
DOI: 10.1074/jbc.M403734200

Experimental method

SOLUTION NMR