30UN
Crystal structure of Homoserine O-succinyltransferase from Cupriavidus Necator
Summary for 30UN
| Entry DOI | 10.2210/pdb30un/pdb |
| Descriptor | Homoserine O-succinyltransferase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | homoserine o-succinyltransferase, amino-acid biosynthesis, methionine biosynthesis, transferase |
| Biological source | Cupriavidus necator |
| Total number of polymer chains | 2 |
| Total formula weight | 89692.02 |
| Authors | Oerlemans, R.,Meier, H.P.F.,Municino, E.,Groves, M.R.,Schmidt, S. (deposition date: 2026-05-13, release date: 2026-11-04) |
| Primary citation | Meier, H.P.F.,Oerlemans, R.,Terholsen, H.,Groves, M.R.,Lauterbach, L.,Schmidt, S. Characterization and Crystal Structure Elucidation of the l-Homoserine O-Succinyltransferase MetXS From Cupriavidus necator H16. Chembiochem, 27:e70564-e70564, 2026 Cited by PubMed Abstract: Among the promising microbial platforms to produce value-added products from CO, chemolithoautotrophic bacteria, such as Cupriavidus necator H16 (C. necator), stand out due to their ability to fix CO via the Calvin-Benson-Bassham (CBB) cycle. Although C. necator has been extensively studied as a biotechnological production host, several of its biosynthetic pathways remain incompletely characterized at the biochemical level. This includes l-methionine biosynthesis, for which genome-based functional annotations of key enzymes have not been validated experimentally. In this study, we identified and characterized CnMetXS, a homoserine O-succinyltransferase involved in l-methionine biosynthesis in C. necator. Biochemical characterization demonstrated that CnMetXS catalyzes the transsuccinylation of l-homoserine to O-succinyl-l-homoserine but exhibits no transacetylase activity. Additionally, we determined the apo crystal structure of CnMetXS at 1.86 Å resolution, revealing a homodimer with a MetX-G2 active-site architecture and distinct conformations of the active-site lid region. Structural analysis and docking suggest that Arg335 stabilizes the succinylated enzyme intermediate and explains the observed succinyl-CoA specificity. Together, these results establish the function of CnMetXS and pave the way for metabolic engineering strategies to produce l-methionine in C. necator. PubMed: 42902934DOI: 10.1002/cbic.70564 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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