8TQF
Crystal structure of Soybean SHMT8 in complex with PLP-glycine and diglutamylated 5-formyltetrahydrofolate
Summary for 8TQF
| Entry DOI | 10.2210/pdb8tqf/pdb |
| Descriptor | Serine hydroxymethyltransferase, N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE], 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | complex, enzyme, soybean, transferase |
| Biological source | Glycine max (soybean) |
| Total number of polymer chains | 4 |
| Total formula weight | 221007.35 |
| Authors | Owuocha, L.F.,Beamer, L.J. (deposition date: 2023-08-07, release date: 2024-08-21, Last modification date: 2025-02-19) |
| Primary citation | Owuocha, L.F.,Mitchum, M.G.,Beamer, L.J. Structural insights into binding of polyglutamylated tetrahydrofolate by serine hydroxymethyltransferase 8 from soybean. Front Plant Sci, 15:1451839-1451839, 2024 Cited by PubMed Abstract: Tetrahydrofolate and its derivatives participate in one-carbon transfer reactions in all organisms. The cellular form of tetrahydrofolate (THF) is modified by multiple glutamate residues and polyglutamylation plays a key role in organellar and cellular folate homeostasis. In addition, polyglutamylation of THF is known to increase the binding affinity to enzymes in the folate cycle, many of which can utilize polyglutamylated THF as a substrate. Here, we use X-ray crystallography to provide a high-resolution view of interactions between the enzyme serine hydroxymethyltransferase (SHMT), which provides one carbon precursors for the folate cycle, and a polyglutamylated form of THF. Our 1.7 Å crystal structure of soybean SHMT8 in complex with diglutamylated 5-formyl-THF reveals, for the first time, a structural rearrangement of a loop at the entrance to the folate binding site accompanied by the formation of novel specific interactions between the enzyme and the diglutamyl tail of the ligand. Biochemical assays show that additional glutamate moieties on the folate ligand increase both enzyme stability and binding affinity. Together these studies provide new information on SHMT structure and function and inform the design of anti-folate agents. PubMed: 39224855DOI: 10.3389/fpls.2024.1451839 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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