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. Issue 4 (28th February 2015)

• Record Type: Journal Article
• Authors: Lee, Sang Jae; Lee, Kyu‐Yeon; Lee, Ki‐Young; Kim, Dong‐Gyun; Kim, Soon‐Jong; Lee, Bong‐Jin
• Is Part Of: Proteins. Volume 83:Issue 4(2015)
• Page Start: 781
• Page End: 788
• Publication Date: 2015-02-28
• Subjects: Staphylococcus aureus -- YwpF -- SAV2097 -- type VI secretion system (T6SS) proteins; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.24774
• Languages: English
• ISSNs: 0887-3585

Abstract

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. Proteins 2015; 83:781–788. © 2015 Wiley Periodicals, Inc.