Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments

Thierry Izore, Ramona Duman, Danguole Kureisaite-Ciziene, Jan Lowe

Research output: Contribution to journalArticleResearchpeer-review

16 Citations (Scopus)

Abstract

Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.
Original languageEnglish
Pages (from-to)776-782
Number of pages7
JournalFEBS Letters
Volume588
Issue number5
DOIs
Publication statusPublished - 3 Mar 2014
Externally publishedYes

Keywords

  • Actin
  • Bacterial cytoskeleton
  • Crenarchaea
  • Cytomotive filament
  • Helical filament
  • MreB

Cite this

Izore, Thierry ; Duman, Ramona ; Kureisaite-Ciziene, Danguole ; Lowe, Jan. / Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments. In: FEBS Letters. 2014 ; Vol. 588, No. 5. pp. 776-782.
@article{a9463012efda491c802cf2f89f56ef33,
title = "Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments",
abstract = "Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 {\AA} resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 {\AA}. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 {\AA}. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.",
keywords = "Actin, Bacterial cytoskeleton, Crenarchaea, Cytomotive filament, Helical filament, MreB",
author = "Thierry Izore and Ramona Duman and Danguole Kureisaite-Ciziene and Jan Lowe",
year = "2014",
month = "3",
day = "3",
doi = "10.1016/j.febslet.2014.01.029",
language = "English",
volume = "588",
pages = "776--782",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "5",

}

Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments. / Izore, Thierry; Duman, Ramona; Kureisaite-Ciziene, Danguole; Lowe, Jan.

In: FEBS Letters, Vol. 588, No. 5, 03.03.2014, p. 776-782.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments

AU - Izore, Thierry

AU - Duman, Ramona

AU - Kureisaite-Ciziene, Danguole

AU - Lowe, Jan

PY - 2014/3/3

Y1 - 2014/3/3

N2 - Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.

AB - Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.

KW - Actin

KW - Bacterial cytoskeleton

KW - Crenarchaea

KW - Cytomotive filament

KW - Helical filament

KW - MreB

UR - http://www.scopus.com/inward/record.url?scp=84896709336&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2014.01.029

DO - 10.1016/j.febslet.2014.01.029

M3 - Article

VL - 588

SP - 776

EP - 782

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 5

ER -