4QXZ
Crystal structure of a hypothetical protein from Staphylococcus aureus
Summary for 4QXZ
| Entry DOI | 10.2210/pdb4qxz/pdb |
| Descriptor | Uncharacterized protein (2 entities in total) |
| Functional Keywords | beta-barrel, unknown function |
| Biological source | Staphylococcus aureus subsp. aureus Mu50 |
| Total number of polymer chains | 2 |
| Total formula weight | 38657.75 |
| Authors | Lee, B.-J.,Lee, S.J.,Lee, K.-Y. (deposition date: 2014-07-23, release date: 2015-06-10, Last modification date: 2024-03-20) |
| Primary citation | Lee, S.J.,Lee, K.Y.,Lee, K.Y.,Kim, D.G.,Kim, S.J.,Lee, B.J. 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. Proteins, 83:781-788, 2015 Cited by PubMed 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. PubMed: 25663006DOI: 10.1002/prot.24774 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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