Crystal structure of the GDP-bound GTPase Era from Staphylococcus aureus.

30S biogenesis Bacterial ribosomal maturation factor Era GTPase Ribosome Staphylococcus aureus Translation

Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
18 Oct 2024
Historique:
received: 11 10 2024
accepted: 17 10 2024
medline: 21 10 2024
pubmed: 21 10 2024
entrez: 21 10 2024
Statut: aheadofprint

Résumé

GTPase Era from Staphylococcus aureus belongs to the TRAFAC superfamily of the TrmE-Era-EngA-EngB-Septin-like GTPases class and plays a significant role in the vital activity of this pathogenic microorganism as a maturation factor of the 30S ribosome subunit. However, the functions of this protein are not fully understood, making it a promising object for further study. Here, the 2.76 Å resolution crystal structure of Staphylococcus aureus Era in complex with GDP is presented. Structural comparison with other GTP-bound and GDP-bound homologous proteins, GTPase domain and the KH domain revealed a mutual orientation in S. aureus which has not been described before. The GDP-bound Era structure presented here will facilitate efforts to elucidate its interactions with its regulators and lay the foundation for a structure-based search for specific inhibitors.

Identifiants

pubmed: 39432921
pii: S0006-291X(24)01388-3
doi: 10.1016/j.bbrc.2024.150852
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

150852

Informations de copyright

Copyright © 2024 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Konstantin Usachev reports financial support was provided by Russian Science Foundation. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Evelina Klochkova (E)

Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation.

Artem Biktimirov (A)

Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation.

Daut Islamov (D)

Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation.

Anatolii Belousov (A)

Moscow Institute of Physics and Technology, Dolgoprudny 141701, Russian Federation; Sao Carlos Institute of Physics, University of Sao Paulo, poloTErRA, 13563-120, Sao Carlos, São Paolo, Brazil.

Shamil Validov (S)

Federal Research Center «Kazan Scientific Center of Russian Academy of Sciences», Kazan, 420111, Russian Federation.

Marat Yusupov (M)

National Research Centre Kurchatov Institute, Kurchatov Sq. 2, 123182, Moscow, Russian Federation; Institute of Genetics, Molecular and Cellular Biology, CNRS UMR7104, INSERM U964, Universit'e de Strasbourg, Illkirch, F-67400, France.

Konstantin Usachev (K)

Kazan Federal University, 18 Kremlyovskaya St., 420008, Kazan, Russian Federation. Electronic address: k.usachev@kpfu.ru.

Classifications MeSH