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TitleMutation of active site glutamate in serine hydroxymethyltransferase allows trapping a reactive intermediate: a combined neutron and X-ray crystallography study.
Journal, issue, pagesRsc Adv, Vol. 16, Page 22600-22609, Year 2026
Publish dateFeb 12, 2026 (structure data deposition date)
AuthorsDrago, V.N. / Phillips, R.S. / Kovalevsky, A.
External linksRsc Adv / PubMed:42112277
MethodsX-ray diffraction / neutron diffraction
Resolution1.8 - 2.4 Å
Structure data

PDB-10yn:
Joint X-ray/neutron structure of E53Q mutant of Thermus thermophilus serine hydroxymethyltransferase (TthSHMT)
Method: X-RAY DIFFRACTION / NEUTRON DIFFRACTION / Resolution: 2.4 Å

PDB-10zb:
Room-temperature X-ray structure of E53Q mutant of Thermus thermophilus serine hydroxymethyltransferase (TthSHMT) in complex with PLP-L-Ser external aldimine and tetrahydrofolate (THF)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-DOD:
DEUTERATED WATER

ChemComp-ACT:
ACETATE ION

ChemComp-KOU:
(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine

ChemComp-THG:
(6S)-5,6,7,8-TETRAHYDROFOLATE

ChemComp-HOH:
WATER

Source
  • thermus thermophilus (bacteria)
KeywordsTRANSFERASE / homodimer / pyridoxal-5'-phosphate / one-carbon metabolism / inactive mutant / enzyme-substrate complex

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