title: A switch in disulfide linkage during minicollagen assembly in hydra nematocysts or how to assemble a 150-bar-resistant structure.
abstract: Hydra minicollagen, the shortest collagen known, is an important component of the nematocyst wall, which has a very high tensile strength. It has an unusual structure, with small and closely related Cys-rich domains at both ends of its chains. Three chains are trimerized by a central collagenous domain. Polyhydroxyproline helices connect the Cys-rich domains with the collagenous domain. The minicollagen precursor contains three internal disulfide bridges in each Cys-rich domain and no disulfide bridges between chains of the same trimeric molecule or between different molecules. Biochemical and structural evidence as well as confocal immunofluorescence microscopy points to disulfide-mediated assembly during maturation of nematocysts.
authors.affiliation: Department of Biophysical Chemistry, Biozentrum, University of Basel, Switzerland.
authors.forename: Suat
authors.initials: S
authors.lastname: Ozbek
authors.forename: Ulrike
authors.initials: U
authors.lastname: Engel
authors.forename: Jürgen
authors.initials: J
authors.lastname: Engel
mesh_terms: D000818:Animals; D003094:Collagen / Q000737:chemistry*; D003553:Cystine / Q000737:chemistry; D019281:Dimerization; D004220:Disulfides; D006829:Hydra / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D004220:Disulfides; D003553:Cystine; D003094:Collagen