Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall

Sebastian Meier, Pernille Rose Jensen, Patrizia Adamczyk, Hans Peter Bachinger, Thomas W. Holstein, Juergen Engel, Suat Oezbek, Stephan Grzesiek

Research output: Contribution to journalJournal articleResearchpeer-review


The nematocyst wall of cnidarians is a unique biomaterial that withstands extreme osmotic pressures, allowing an ultrafast discharge of the nematocyst capsules. Assembly of the highly robust nernatocyst wall is achieved by covalent linkage of cysteine-rich domains (CRDs) from two main protein components, minicollagens and nematocyst outer wall antigen (NOWA). The bipolar minicollagens have different disulfide patterns and topologies in their N and C-terminal CRDs. The functional significance of this polarity has been elusive. Here, we show by NMR structural analysis that all representative cysteine-rich domains of NOWA are structurally related to N-terminal minicollagen domains. Natural sequence insertions in NOWA CRDs have very little effect on the tightly knit domain structures, nor do they preclude the efficient folding to a single native conformation. The different folds in NOWA CRDs and the atypical C-terminal minicollagen domain on the other hand can be directly related to different conformational preferences in the reduced states. Ultrastructural analysis in conjunction with aggregation studies argues for an association between the similar NOWA and N-terminal minicollagen domains in early stages of the nernatocyst wall assembly, which is followed by the controlled association between the unusual structures of C-terminal minicollagen domains. (c) 2007 Elsevier Ltd. All rights reserved.
Original languageEnglish
JournalJournal of Molecular Biology
Issue number3
Pages (from-to)718-728
Publication statusPublished - 2007
Externally publishedYes


  • Amino Acid Sequence
  • Animals
  • Cell Wall
  • Cnidaria
  • Collagen
  • Cysteine
  • Evolution, Molecular
  • Glycoproteins
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Folding
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Structure-Activity Relationship
  • 9007-34-5 Collagen
  • K848JZ4886 Cysteine
  • antigen
  • collagen
  • cysteine
  • disulfide
  • amino terminal sequence
  • article
  • coelenterate
  • nonhuman
  • nuclear magnetic resonance spectroscopy
  • osmotic pressure
  • priority journal
  • protein aggregation
  • protein domain
  • protein folding
  • sequence analysis
  • structure analysis
  • ultrastructure
  • conformational diversity
  • cysteine-rich
  • dihedral angle preference
  • molecular evolution
  • NMR structure
  • CRD; cysteine-rich domain
  • NW8r; eighth CRD of NOWA
  • Mcol1hN; N-terminal CRD of minicollagen 1 from Hydra
  • Mcol1hC; C-terminal CRD of minicollagen 1 from Hydra
  • RDC; residual dipolar coupling
  • NOWA; nematocyst outer wall antigen
  • CROD; cysteine-rich octarepeat domain of NOWA
  • NW1r; first CRD of NOWA
  • NW6r; sixth CRD of NOWA
  • NOE; nuclear Overhauser effect
  • TCEP; Tris(2-carboxyethyl)-phosphine
  • GSH; reduced glutathione
  • GSSG; oxidized glutathione
  • HSQC; heteronuclear single quantum correlation
  • indel; insertion/deletion
  • domain sequence structure
  • cysteine-rich domain
  • 04500, Mathematical biology and statistical methods
  • 10060, Biochemistry studies - General
  • Computational Biology
  • nematocyst wall
  • structure-function analysis mathematical and computer techniques
  • Biochemistry and Molecular Biophysics
  • Mathematical Biology


Dive into the research topics of 'Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall'. Together they form a unique fingerprint.

Cite this