Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation

Sebastian Meier, D. Haussinger, E. Pokidysheva, HP Bachinger, S. Grzesiek

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageEnglish
JournalFEBS Letters
Volume569
Issue number1-3
Pages (from-to)112-116
Number of pages5
ISSN0014-5793
DOIs
Publication statusPublished - 2004
Externally publishedYes

Keywords

  • Amino Acid Sequence
  • Animals
  • Collagen
  • Cysteine
  • Disulfides
  • Glutathione
  • Glutathione Disulfide
  • Hydra
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • 9007-34-5 Collagen
  • GAN16C9B8O Glutathione
  • K848JZ4886 Cysteine
  • ULW86O013H Glutathione Disulfide
  • collagen
  • cysteine
  • glutathione
  • proline
  • accuracy
  • amino acid sequence
  • analytic method
  • article
  • carboxy terminal sequence
  • coelenterate
  • disulfide bond
  • nonhuman
  • nuclear magnetic resonance
  • oxidation
  • oxidation reduction reaction
  • priority journal
  • protein domain
  • protein folding
  • protein structure
  • reduction
  • titrimetry
  • Disulfide bond
  • Heteronuclear NMR
  • Nematocyst
  • Residual dipolar coupling
  • BIOCHEMISTRY
  • BIOPHYSICS
  • CELL
  • ENDOPLASMIC-RETICULUM
  • PROTEIN-STRUCTURE
  • CHEMICAL-SHIFT
  • NEMATOCYSTS
  • GLUTATHIONE
  • ALIGNMENT
  • COLLAGENS
  • LINKAGE
  • SYSTEM
  • SWITCH
  • nematocyst
  • residual dipolar coupling
  • disulfide bond formation
  • Invertebrata Animalia (Animals, Invertebrates) - Cnidaria [41000] Hydra genus
  • cysteine 52-90-4Q, 3374-22-9Q
  • glutathione 70-18-8
  • proline 147-85-3Q, 609-36-9Q
  • 10060, Biochemistry studies - General
  • 10064, Biochemistry studies - Proteins, peptides and amino acids
  • 64008, Invertebrata: comparative, experimental morphology, physiology and pathology - Cnidaria
  • NMR laboratory techniques, spectrum analysis techniques
  • Biochemistry and Molecular Biophysics
  • Methods and Techniques

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