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Publication Abstract from PubMed

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-A resolution. The YwpF structure consists of two regions: an N-terminal core beta-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.

Crystal structure of YwpF from Staphylococcus aureus reveals its architecture comprised of a beta-barrel core domain resembling type VI secretion system proteins and a two-helix pair.,Lee SJ, Lee KY, Lee KY, Kim DG, Kim SJ, Lee BJ Proteins. 2015 Apr;83(4):781-8. doi: 10.1002/prot.24774. Epub 2015 Feb 28. PMID:25663006^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.