Structural highlights
Function
ERA_STAA8 An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.[HAMAP-Rule:MF_00367]
Publication Abstract from PubMed
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 A 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.
Crystal structure of the GDP-bound GTPase Era from Staphylococcus aureus.,Klochkova E, Biktimirov A, Islamov D, Belousov A, Validov S, Yusupov M, Usachev K Biochem Biophys Res Commun. 2024 Nov 26;735:150852. doi: , 10.1016/j.bbrc.2024.150852. Epub 2024 Oct 18. PMID:39432921[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klochkova E, Biktimirov A, Islamov D, Belousov A, Validov S, Yusupov M, Usachev K. Crystal structure of the GDP-bound GTPase Era from Staphylococcus aureus. Biochem Biophys Res Commun. 2024 Nov 26;735:150852. PMID:39432921 doi:10.1016/j.bbrc.2024.150852
