8YRC
Chlorinated YabJ from Staphylococcus aureus
Summary for 8YRC
Entry DOI | 10.2210/pdb8yrc/pdb |
Related | 5YU2 |
Descriptor | Translation initiation inhibitor homologue, OXYGEN ATOM, SODIUM ION, ... (5 entities in total) |
Functional Keywords | ribonuclease, stress-response protein, structural protein |
Biological source | Staphylococcus aureus subsp. aureus Mu50 |
Total number of polymer chains | 3 |
Total formula weight | 42903.60 |
Authors | |
Primary citation | Jeong, C.,Kim, H.J. YabJ from Staphylococcus aureus entraps chlorides within its pocket. Biochem.Biophys.Res.Commun., 710:149892-149892, 2024 Cited by PubMed Abstract: Chlorination is a potent disinfectant against various microorganisms, including bacteria and viruses, by inducing protein modifications and functional changes. Chlorine, in the form of sodium hypochlorite, stands out as the predominant sanitizer choice due to its cost-effectiveness and powerful antimicrobial properties. Upon exposure to chlorination, proteins undergo modifications, with amino acids experiencing alterations through the attachment of chloride or oxygen atoms. These modifications lead to shifts in protein function and the modulation of downstream signaling pathways, ultimately resulting in a bactericidal effect. However, certain survival proteins, such as chaperones or transcription factors, aid organisms in overcoming harsh chlorination conditions. The expression of YabJ, a highly conserved protein from Staphylococcus aureus, is regulated by a stress-activated sigma factor called sigma B (σB). This research revealed that S. aureus YabJ maintains its structural integrity even under intense chlorination conditions and harbors sodium hypochlorite molecules within its surface pocket. Notably, the pocket of S. aureus YabJ is primarily composed of amino acids less susceptible to chlorination-induced damage, rendering it resistant to such effects. This study elucidates how S. aureus YabJ evades the detrimental effects of chlorination and highlights its role in sequestering sodium hypochlorite within its structure. Consequently, this process enhances resilience and facilitates adaptation to challenging environmental conditions. PubMed: 38581951DOI: 10.1016/j.bbrc.2024.149892 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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