Structure formation in the C terminus of type III collagen guides disulfide cross-linking.

Boudko SP, Engel J
J Mol Biol. 2004 335 (5): 1289-97

PMID: 14729344 · DOI:10.1016/j.jmb.2003.11.054

In type III collagen the main triple-helical domain is followed by a disulfide knot and the C-terminal propeptide, which are both essential for nucleation, stabilization and registration of the triple helix. We demonstrate that oxidative inter-chain disulfide bridging does not occur between the knot sequences GlyProCysCysGly of dissociated randomly coiled chains. N-terminal fusion of the obligatory trimeric domain of mini-fibritin is able to direct this process efficiently, demonstrating a folded precursor mechanism in which the thiol groups have to be properly placed for the formation of native disulfide bonds. The natural C-propeptide domain may act in a similar way as the mini-fibritin domain. After disulfide linkage and triple-helix formation the catalyzing mini-fibritin domain was removed by thrombin cleavage. In this way a short but stable triple-helical collagen fragment was expressed in Escherichia coli for structural and functional studies.

MeSH Terms (14)

Calorimetry, Differential Scanning Circular Dichroism Collagen Type III Cross-Linking Reagents Disulfides Escherichia coli Mass Spectrometry Oxidation-Reduction Peptide Fragments Protein Conformation Protein Folding Recombinant Proteins Ultracentrifugation Viral Proteins

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