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

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 resolu...

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Autores principales: Izoré, Thierry, Duman, Ramona, Kureisaite-Ciziene, Danguole, Löwe, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons Ltd 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158420/
https://www.ncbi.nlm.nih.gov/pubmed/24486010
http://dx.doi.org/10.1016/j.febslet.2014.01.029
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author Izoré, Thierry
Duman, Ramona
Kureisaite-Ciziene, Danguole
Löwe, Jan
author_facet Izoré, Thierry
Duman, Ramona
Kureisaite-Ciziene, Danguole
Löwe, Jan
author_sort Izoré, Thierry
collection PubMed
description 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.
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spelling pubmed-41584202014-09-10 Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments Izoré, Thierry Duman, Ramona Kureisaite-Ciziene, Danguole Löwe, Jan FEBS Lett Article 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. John Wiley & Sons Ltd 2014-03-03 /pmc/articles/PMC4158420/ /pubmed/24486010 http://dx.doi.org/10.1016/j.febslet.2014.01.029 Text en © 2014 Elsevier B.V. on behalf of the Federation of European Biochemical Societies. All rights reserved. https://creativecommons.org/licenses/by/3.0/This work is licensed under a Creative Commons Attribution 3.0 Unported License (https://creativecommons.org/licenses/by/3.0/) .
spellingShingle Article
Izoré, Thierry
Duman, Ramona
Kureisaite-Ciziene, Danguole
Löwe, Jan
Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title_full Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title_fullStr Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title_full_unstemmed Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title_short Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
title_sort crenactin from pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158420/
https://www.ncbi.nlm.nih.gov/pubmed/24486010
http://dx.doi.org/10.1016/j.febslet.2014.01.029
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