title: Crystal structure of YwpF from Staphylococcus aureus reveals its architecture comprised of a β-barrel core domain resembling type VI secretion system proteins and a two-helix pair.
abstract: The ywpF gene (SAV2097) of the Staphylococcus aureus strain Mu50 encodes the YwpF protein, which may play a role in antibiotic resistance. Here, we report the first crystal structure of the YwpF superfamily from S. aureus at 2.5-Å resolution. The YwpF structure consists of two regions: an N-terminal core β-barrel domain that shows structural similarity to type VI secretion system (T6SS) proteins (e.g., Hcp1, Hcp3, and EvpC) and a C-terminal two-helix pair. Although the monomer structure of S. aureus YwpF resembles those of T6SS proteins, the dimer/tetramer model of S. aureus YwpF is distinct from the functionally important hexameric ring of T6SS proteins. We therefore suggest that the S. aureus YwpF may have a different function compared to T6SS proteins.
authors: The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-Gu, Seoul, 151-742, Korea.
authors: Sang Jae
authors: SJ
authors: Lee
authors: Kyu-Yeon
authors: KY
authors: Lee
authors: Ki-Young
authors: KY
authors: Lee
authors: Dong-Gyun
authors: DG
authors: Kim
authors: Soon-Jong
authors: SJ
authors: Kim
authors: Bong-Jin
authors: BJ
authors: Lee
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D008958:Models, Molecular; D021122:Protein Subunits / Q000737:chemistry; D013211:Staphylococcus aureus / Q000737:chemistry*; D000069376:Type VI Secretion Systems; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D000069376:Type VI Secretion Systems
keywords: SAV2097; Staphylococcus aureus; YwpF; type VI secretion system (T6SS) proteins