8U7J
Crystal Structure of Staphylococcus aureus PLP synthase complex
Summary for 8U7J
| Entry DOI | 10.2210/pdb8u7j/pdb |
| Descriptor | Pyridoxal 5'-phosphate synthase subunit PdxS, Pyridoxal 5'-phosphate synthase subunit PdxT, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | plp synthase complex, pdx1-pdx2, staphylococcus aureus, biosynthetic protein |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 24 |
| Total formula weight | 637919.23 |
| Authors | Barra, A.L.C.,Brognaro, H.,Betzel, C.,Nascimento, A.S. (deposition date: 2023-09-15, release date: 2024-07-24, Last modification date: 2024-07-31) |
| Primary citation | Barra, A.L.C.,Ullah, N.,Brognaro, H.,Gutierrez, R.F.,Wrenger, C.,Betzel, C.,Nascimento, A.S. Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface. J.Biol.Chem., 300:107404-107404, 2024 Cited by PubMed Abstract: Infectious diseases are a significant cause of death, and recent studies estimate that common bacterial infectious diseases were responsible for 13.6% of all global deaths in 2019. Among the most significant bacterial pathogens is Staphylococcus aureus, accounting for more than 1.1 million deaths worldwide in 2019. Vitamin biosynthesis has been proposed as a promising target for antibacterial therapy. Here, we investigated the biochemical, structural, and dynamic properties of the enzyme complex responsible for vitamin B6 (pyridoxal 5-phosphate, PLP) biosynthesis in S. aureus, which comprises enzymes SaPdx1 and SaPdx2. The crystal structure of the 24-mer complex of SaPdx1-SaPdx2 enzymes indicated that the S. aureus PLP synthase complex forms a highly dynamic assembly with transient interaction between the enzymes. Solution scattering data indicated that SaPdx2 typically binds to SaPdx1 at a substoichiometric ratio. We propose a structure-based view of the PLP synthesis mechanism initiated with the assembly of SaPLP synthase complex that proceeds in a highly dynamic interaction between Pdx1 and Pdx2. This interface interaction can be further explored as a potentially druggable site for the design of new antibiotics. PubMed: 38782204DOI: 10.1016/j.jbc.2024.107404 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
Download full validation report
