Crystal structure of GTPase YsxC from Staphylococcus aureus.
Fiche publication
Date publication
janvier 2024
Journal
Biochemical and biophysical research communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat
Tous les auteurs :
Biktimirov A, Islamov D, Fatkhullin B, Lazarenko V, Validov S, Yusupov M, Usachev K
Lien Pubmed
Résumé
The YsxC protein from Staphylococcus aureus is a GTP-binding protein from the TRAFAC superfamily of the TrmE-Era-EngA-EngB-Septin-like GTPase class, EngB family of GTPases. Recent structural and biochemical studies of YsxC function show that it is an integral part of the pathogenic microorganism life cycle, as it is involved in the assembly of the large 50S ribosomal subunit. Structural studies of this protein with its specific functional features make it an attractive target for further development of new selective antimicrobials. In this study, we cloned the ysxC protein gene from S. aureus, overexpressed the protein in E. coli, and subsequently purified and crystallized it. Protein crystals were successfully grown using the vapor diffusion method, yielding diffraction data with a resolution of up to 2 Å. Comparative analysis of the structure of SaYsxC with known three-dimensional structures of homologs from other microorganisms showed the presence of structural differences for the apo form.
Mots clés
Crystallography, GTPase, Staphylococcus aureus, X-ray, YsxC
Référence
Biochem Biophys Res Commun. 2024 01 17;699:149545