The structure of the Cys-rich terminal domain of hydra minicollagen, which is involved in disulfide networks of the nematocyst wall

E. Pokidysheva, AG Milbradt, Sebastian Meier, C. Renner, D. Haussinger, HP Bachinger, L. Moroder, S. Grzesiek, TW Holstein, S. Ozbek, J. Engel

Research output: Contribution to journalJournal articleResearchpeer-review

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 (CXXXCXXXCXXXCXXXCC). 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 H-1 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 (Cys(2)-Cys(18), Cys(6)-Cys(14), and Cys(10)-Cys(19)) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume279
Issue number29
Pages (from-to)30395-30401
ISSN0021-9258
DOIs
Publication statusPublished - 2004
Externally publishedYes

Keywords

  • MOLECULAR structure
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Collagen
  • Cysteine
  • Cystine
  • Disulfides
  • Glycine
  • Hydra
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Models, Molecular
  • Molecular Sequence Data
  • Oxygen
  • Peptides
  • Protein Conformation
  • Protein Folding
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Time Factors
  • Ultracentrifugation
  • 48TCX9A1VT Cystine
  • 9007-34-5 Collagen
  • K848JZ4886 Cysteine
  • S88TT14065 Oxygen
  • TE7660XO1C Glycine
  • Amino acids
  • Cells
  • Chemical bonds
  • Molecular structure
  • collagen
  • cysteine
  • hydroxyproline
  • proline
  • article
  • carboxy terminal sequence
  • cell wall
  • coelenterate
  • concentration (parameters)
  • disulfide bond
  • nonhuman
  • oxidation
  • polymerization
  • priority journal
  • proton nuclear magnetic resonance
  • Coelenterata
  • Invertebrata
  • Nematocysts
  • Structural motifs
  • T
  • X
  • BIOCHEMISTRY
  • BASEMENT-MEMBRANE
  • IV COLLAGEN
  • PROTEIN
  • BONDS
  • LINKAGE
  • SYSTEM
  • SWITCH
  • CORAL
  • disulfide network
  • intermolecular bond
  • intramolecular bond
  • Invertebrata Animalia (Animals, Invertebrates) - Cnidaria [41000] Hydra genus
  • minicollagen-1
  • 02502, Cytology - General
  • 02506, Cytology - Animal
  • 10060, Biochemistry studies - General
  • 64008, Invertebrata: comparative, experimental morphology, physiology and pathology - Cnidaria
  • proton nuclear magnetic resonance laboratory techniques, spectrum analysis techniques
  • Biochemistry and Molecular Biophysics
  • Cell Biology

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