7OFN

NMR solution structure of the SYLF domain of Burkholderia pseudomallei BPSL1445

Summary for 7OFN

• Entry DOI: 10.2210/pdb7ofn/pdb
• NMR Information: BMRB: 25387
• Descriptor: Lipoprotein (1 entity in total)
• Functional Keywords: burkholderia pseudomallei lipoprotein sylf domain beta berrel, lipid binding protein
• Biological source: Burkholderia pseudomallei (Pseudomonas pseudomallei)
• Total number of polymer chains: 1
• Total formula weight: 16536.77

Authors

Quilici, G.,Berardi, A.,Musco, G. (deposition date: 2021-05-05, release date: 2021-12-29, Last modification date: 2024-06-19)

Primary citation

Quilici, G.,Berardi, A.,Fabris, C.,Ghitti, M.,Punta, M.,Gourlay, L.J.,Bolognesi, M.,Musco, G.
Solution Structure of the BPSL1445 Protein of Burkholderia pseudomallei Reveals the SYLF Domain Three-Dimensional Fold.
Acs Chem.Biol., 17:230-239, 2022

PubMed 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 , 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.

PubMed: 34968022
DOI: 10.1021/acschembio.1c00886

Experimental method

SOLUTION NMR