Structural organization of flagellin

Ferenc Vonderviszt, Hatsuho Uedaira, Shun Ichi Kidokoro, Keiichi Namba

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

The terminal regions of flagellin fromSalmonella typhimurium have been reported to be disordered in solution, whereas the central part of the molecule contains protease-resistant, compact structural units. Here, conformational properties of flagellin and its proteolytic fragments were investigated and compared to characterize the domain organization and secondary structure of flagellin. Deconvolution analysis of the calorimetric melting profiles of flagellin and its fragments suggests that flagellin is composed of three co-operative units or domains. The central part of the molecule, residues 179 to 418, consists of two domains (G1 and G2), whereas the third domain (G3) is discontinuous, constructed from segments 67 to 178 and 419 to 448. Secondary structure prediction and analysis of far-ultraviolet circular dichroic spectra have revealed that G1 and G2 consist predominantly of β-structure with a little α-helical content. G3 contains almost equal amounts of α and β-structure, while in the terminal parts of flagellin the ordered secondary structure seems to be entirely α-helical.

Original languageEnglish
Pages (from-to)97-104
Number of pages8
JournalJournal of molecular biology
Volume214
Issue number1
DOIs
Publication statusPublished - Jul 5 1990

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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