5T73

Crystal structure of S.aureus glyceraldehyde-3-phosphate-dehydrogenase (Gap) containing oxidized Cys151

Summary for 5T73

• Entry DOI: 10.2210/pdb5t73/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase 1, SODIUM ION (3 entities in total)
• Functional Keywords: glycolysis, oxidoreductase, oxidation
• Biological source: Staphylococcus aureus (strain MRSA252)
• Cellular location: Cytoplasm : Q6GIL8
• Total number of polymer chains: 4
• Total formula weight: 145658.97

Authors

Pietrzyk-Brzezinska, A.J.,Wahl, M.C. (deposition date: 2016-09-02, release date: 2016-12-28, Last modification date: 2024-01-17)

Primary citation

Imber, M.,Huyen, N.T.T.,Pietrzyk-Brzezinska, A.J.,Loi, V.V.,Hillion, M.,Bernhardt, J.,Tharichen, L.,Kolsek, K.,Saleh, M.,Hamilton, C.J.,Adrian, L.,Grater, F.,Wahl, M.C.,Antelmann, H.
Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.
Antioxid. Redox Signal., 28:410-430, 2018

PubMed Abstract: Bacillithiol (BSH) is the major low-molecular-weight thiol of the human pathogen Staphylococcus aureus. In this study, we used OxICAT and Voronoi redox treemaps to quantify hypochlorite-sensitive protein thiols in S. aureus USA300 and analyzed the role of BSH in protein S-bacillithiolation.

PubMed: 27967218
DOI: 10.1089/ars.2016.6897

Experimental method

X-RAY DIFFRACTION (2.599 Å)