ArticleThe Journal of biological chemistry2019
A flap motif in human serine hydroxymethyltransferase is important for structural stabilization, ligand binding, and control of product release.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Oligomeric defects in soybean serine hydroxymethyltransferase 8: tetramer destabilization by A149T and other variants associated with soybean cyst nematode resistance.The FEBS journal · 2026Article
- Comparative binding and activity analysis of known serine hydroxymethyltransferase inhibitors in biochemical assays.RSC advances · 2026Article
- Universality of critical active site glutamate as an acid-base catalyst in serine hydroxymethyltransferase function.Chemical science · 2024Article
- Design of electron-donating group substituted 2-PAM analogs as antidotes for organophosphate insecticide poisoning.RSC advances · 2023Article
- In Silico and In Vitro Potential of FDA-Approved Drugs for Antimalarial Drug Repurposing againstACS omega · 2023Article
- Characterization of thermostable serine hydroxymethyltransferase for β-hydroxy amino acids synthesis.Amino acids · 2023Article
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- SHMT2 expression as a diagnostic and prognostic marker for thyroid cancer.Endocrine connections · 2021Article
- Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.The Journal of biological chemistry · 2020Article
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Authors and funding
12 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human cytosolic serine hydroxymethyltransferase (hcSHMT) is a promising target for anticancer chemotherapy and contains a flexible "flap motif" whose function is yet unknown. Here, using size-exclusion chromatography, analytical ultracentrifugation, small-angle X-ray scattering (SAXS), molecular dynamics (MD) simulations, and ligand-binding and enzyme-kinetic analyses, we studied the functional roles of the flap motif by comparing WT hcSHMT with a flap-deleted variant (hcSHMT/Δflap). We found that deletion of the flap results in a mixture of apo-dimers and holo-tetramers, whereas the WT was mostly in the tetrameric form. MD simulations indicated that the flap stabilizes structural compactness and thereby enhances oligomerization. The hcSHMT/Δflap variant exhibited different catalytic properties in (6
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