Solution Structure of the BPSL1445 Protein of Burkholderia pseudomallei Reveals the SYLF Domain Three-Dimensional Fold
Articolo
Data di Pubblicazione:
2022
Citazione:
Solution Structure of the BPSL1445 Protein of Burkholderia pseudomallei Reveals the SYLF Domain Three-Dimensional Fold / G. Quilici, A. Berardi, C. Fabris, M. Ghitti, M. Punta, L.J. Gourlay, M. Bolognesi, G. Musco. - In: ACS CHEMICAL BIOLOGY. - ISSN 1554-8929. - 17:1(2022 Jan), pp. 230-239. [10.1021/acschembio.1c00886]
Abstract:
The SYLF domain is an evolutionary conserved protein domain with phosphatidylinositol binding ability, whose three-dimensional structure is unknown. Here, we present the solution structure and the dynamics characterization of the SYLF domain of the bacterial BPSL1445 protein. BPSL1445 is a seroreactive antigen and a diagnostic marker of Burkholderia pseudomallei, the etiological agent of melioidosis, a severe infectious disease in the tropics. The BPSL1445 SYLF domain (BPSL1445-SYLF) consists of a β-barrel core, with two flexible loops protruding out of the barrel and three helices packing on its surface. Our structure allows for a more precise definition of the boundaries of the SYLF domain compared to the previously reported one and suggests common ancestry with bacterial EipA domains. We also demonstrate by phosphatidyl-inositol phosphate arrays and nuclear magnetic resonance titrations that BPSL1445-SYLF weakly interacts with phosphoinositides, thus supporting lipid binding abilities of this domain also in prokaryotes.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
G. Quilici, A. Berardi, C. Fabris, M. Ghitti, M. Punta, L.J. Gourlay, M. Bolognesi, G. Musco
Link alla scheda completa: