8QWA
Adenylosuccinate Synthetase from H. pylori in complex with PLP and IMP
Summary for 8QWA
| Entry DOI | 10.2210/pdb8qwa/pdb |
| Descriptor | Adenylosuccinate synthetase, INOSINIC ACID, PYRIDOXAL-5'-PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | purine salvage pathway, complex with inhibitor, amp precursos synthesis, ligase |
| Biological source | Helicobacter pylori 26695 |
| Total number of polymer chains | 1 |
| Total formula weight | 46593.20 |
| Authors | |
| Primary citation | Wojtys, M.I.,Maksymiuk, W.,Narczyk, M.,Bubic, A.,Asler, I.L.,Krzyzek, P.,Gosciniak, G.,Jagusztyn-Krynicka, E.K.,Bzowska, A. Vitamin B6 inhibits activity of Helicobacter pylori adenylosuccinate synthetase and growth of reference and clinical, antibiotic-resistant H. pylori strains. J Enzyme Inhib Med Chem, 39:2372734-2372734, 2024 Cited by PubMed Abstract: The current therapies against gastric pathogen are ineffective in over 20% of patients. Enzymes belonging to the purine salvage pathway are considered as novel drug targets in this pathogen. Therefore, the main aim of the current study was to determine the antibacterial activity of pyridoxal 5'-phosphate (PLP), an active form of vitamin B6, against reference and clinical strains of . Using a broad set of microbiological, physicochemical (UV absorption, LC-MS, X-ray analysis) and experiments, we were able to prove that PLP inhibits adenylosuccinate synthetase (AdSS) from by the competition with GTP (IC ∼30 nM). This behaviour was attributed to formation of a Schiff base with a lysine residue (a covalent bond with Lys322 in the GTP binding site of AdSS) and was potentiated by the presence of vitamin C. This antibacterial activity of PLP gives hope for its future use against . PubMed: 39149761DOI: 10.1080/14756366.2024.2372734 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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