8U9E

Crystal Structure of Staphylococcus aureus Pdx1

Summary for 8U9E

• Entry DOI: 10.2210/pdb8u9e/pdb
• Descriptor: Pyridoxal 5'-phosphate synthase subunit PdxS, 1,2-ETHANEDIOL, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: synthase, vitamin b6 synthase, biosynthetic protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 65098.61

Authors

Barra, A.L.C.,Nascimento, A.S. (deposition date: 2023-09-19, 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

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: 38782204
DOI: 10.1016/j.jbc.2024.107404

Experimental method

X-RAY DIFFRACTION (3.02 Å)