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Proteins. 2015 Apr;83(4):781-8. doi: 10.1002/prot.24774. Epub 2015 Feb 28.

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.

Author information

1
The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-Gu, Seoul, 151-742, Korea.

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.

KEYWORDS:

SAV2097; Staphylococcus aureus; YwpF; type VI secretion system (T6SS) proteins

PMID:
25663006
DOI:
10.1002/prot.24774
[Indexed for MEDLINE]

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