Terminal disorder

A common structural feature of the axial proteins of bacterial flagellum?

F. Vonderviszt, Rieko Ishima, Kazuyuki Akasaka, Shin Ichi Aizawa

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

We report, based on proteolytic experiments and high resolution 1H nuclear magnetic resonance studies that the terminal regions of the monomeric hook protein are highly mobile and exposed to the solvent. The disordered parts of the hook protein span approximately the first 70 and the last 30 amino acid residues. Although the amino acid sequences of flagellin and hook protein do not resemble each other at all, both proteins have now been shown to contain large disordered terminal regions. Sequential similarities of flagellin and hook protein, especially near the NH2 and COOH termini. to other axial components of bacterial flagellum suggest that terminal disorder may be a common structural feature of the axial proteins of the bacterial flagellum.

Original languageEnglish
Pages (from-to)575-579
Number of pages5
JournalJournal of Molecular Biology
Volume226
Issue number3
DOIs
Publication statusPublished - Aug 5 1992

Fingerprint

Bacterial Proteins
Flagella
Flagellin
Proteins
Amino Acid Sequence
Magnetic Resonance Spectroscopy
Amino Acids

Keywords

  • bacterial flagellar filament
  • disordered regions
  • flagellin
  • hook protein
  • self-assembly

ASJC Scopus subject areas

  • Virology

Cite this

Terminal disorder : A common structural feature of the axial proteins of bacterial flagellum? / Vonderviszt, F.; Ishima, Rieko; Akasaka, Kazuyuki; Aizawa, Shin Ichi.

In: Journal of Molecular Biology, Vol. 226, No. 3, 05.08.1992, p. 575-579.

Research output: Contribution to journalArticle

Vonderviszt, F. ; Ishima, Rieko ; Akasaka, Kazuyuki ; Aizawa, Shin Ichi. / Terminal disorder : A common structural feature of the axial proteins of bacterial flagellum?. In: Journal of Molecular Biology. 1992 ; Vol. 226, No. 3. pp. 575-579.
@article{a0a71656a07b4f2eb31800d726bdfc0e,
title = "Terminal disorder: A common structural feature of the axial proteins of bacterial flagellum?",
abstract = "We report, based on proteolytic experiments and high resolution 1H nuclear magnetic resonance studies that the terminal regions of the monomeric hook protein are highly mobile and exposed to the solvent. The disordered parts of the hook protein span approximately the first 70 and the last 30 amino acid residues. Although the amino acid sequences of flagellin and hook protein do not resemble each other at all, both proteins have now been shown to contain large disordered terminal regions. Sequential similarities of flagellin and hook protein, especially near the NH2 and COOH termini. to other axial components of bacterial flagellum suggest that terminal disorder may be a common structural feature of the axial proteins of the bacterial flagellum.",
keywords = "bacterial flagellar filament, disordered regions, flagellin, hook protein, self-assembly",
author = "F. Vonderviszt and Rieko Ishima and Kazuyuki Akasaka and Aizawa, {Shin Ichi}",
year = "1992",
month = "8",
day = "5",
doi = "10.1016/0022-2836(92)90616-R",
language = "English",
volume = "226",
pages = "575--579",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Terminal disorder

T2 - A common structural feature of the axial proteins of bacterial flagellum?

AU - Vonderviszt, F.

AU - Ishima, Rieko

AU - Akasaka, Kazuyuki

AU - Aizawa, Shin Ichi

PY - 1992/8/5

Y1 - 1992/8/5

N2 - We report, based on proteolytic experiments and high resolution 1H nuclear magnetic resonance studies that the terminal regions of the monomeric hook protein are highly mobile and exposed to the solvent. The disordered parts of the hook protein span approximately the first 70 and the last 30 amino acid residues. Although the amino acid sequences of flagellin and hook protein do not resemble each other at all, both proteins have now been shown to contain large disordered terminal regions. Sequential similarities of flagellin and hook protein, especially near the NH2 and COOH termini. to other axial components of bacterial flagellum suggest that terminal disorder may be a common structural feature of the axial proteins of the bacterial flagellum.

AB - We report, based on proteolytic experiments and high resolution 1H nuclear magnetic resonance studies that the terminal regions of the monomeric hook protein are highly mobile and exposed to the solvent. The disordered parts of the hook protein span approximately the first 70 and the last 30 amino acid residues. Although the amino acid sequences of flagellin and hook protein do not resemble each other at all, both proteins have now been shown to contain large disordered terminal regions. Sequential similarities of flagellin and hook protein, especially near the NH2 and COOH termini. to other axial components of bacterial flagellum suggest that terminal disorder may be a common structural feature of the axial proteins of the bacterial flagellum.

KW - bacterial flagellar filament

KW - disordered regions

KW - flagellin

KW - hook protein

KW - self-assembly

UR - http://www.scopus.com/inward/record.url?scp=0026737755&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026737755&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(92)90616-R

DO - 10.1016/0022-2836(92)90616-R

M3 - Article

VL - 226

SP - 575

EP - 579

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -