A switch in disulfide linkage during minicollagen assembly in hydra nematocysts or how to assemble a 150-bar-resistant structure

J Struct Biol. 2002 Jan-Feb;137(1-2):11-4. doi: 10.1006/jsbi.2002.4436.

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Collagen / chemistry*
  • Cystine / chemistry
  • Dimerization
  • Disulfides*
  • Hydra / metabolism
  • Hydra / physiology*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • Disulfides
  • Cystine
  • Collagen