Structure of crenactin, an archaeal actin homologue active at 90°C.
Acta Crystallogr D Biol Crystallogr
; 70(Pt 2): 492-500, 2014 Feb.
Article
em En
| MEDLINE
| ID: mdl-24531483
ABSTRACT
The crystal structure of the archaeal actin, crenactin, from the rod-shaped hyperthermophilic (optimal growth at 90°C) crenarchaeon Pyrobaculum calidifontis is reported at 3.35â
Å resolution. Despite low amino-acid sequence identity, the three-dimensional structure of the protein monomer is highly similar to those of eukaryotic actin and the bacterial MreB protein. Crenactin-specific features are also evident, as well as elements that are shared between crenactin and eukaryotic actin but are not found in MreB. In the crystal, crenactin monomers form right-handed helices, demonstrating that the protein is capable of forming filament-like structures. Monomer interactions in the helix, as well as interactions between crenactin and ADP in the nucleotide-binding pocket, are resolved at the atomic level and compared with those of actin and MreB. The results provide insights into the structural and functional properties of a heat-stable archaeal actin and contribute to the understanding of the evolution of actin-family proteins in the three domains of life.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Actinas
/
Proteínas Arqueais
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Proteínas do Citoesqueleto
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Proteínas de Saccharomyces cerevisiae
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Pyrobaculum
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article