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TitleNeutron diffraction reveals protonation states in pyridoxal-5'-phosphate-free and glycine external aldimine-bound serine hydroxymethyltransferase.
Journal, issue, pagesFebs J., Vol. 293, Page 582-597, Year 2026
Publish dateApr 9, 2025 (structure data deposition date)
AuthorsDrago, V.N. / Blakeley, M.P. / Phillips, R.S. / Kovalevsky, A.
External linksFebs J. / PubMed:40915980
MethodsX-ray diffraction / neutron diffraction
Resolution1.8 - 2.1 Å
Structure data

PDB-9o50:
Room-temperature X-ray structure of Thermus thermophilus SHMT in complex with tetrahydrofolate (THF)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-9o5g:
Room-temperature joint X-ray/Neutron structure of Thermus thermophilus SHMT in complex with PLP-Gly external aldimine and 5-methyl-tetrahydrofolate (5MTHF)
Method: X-RAY DIFFRACTION / NEUTRON DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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

ChemComp-HOH:
WATER

ChemComp-PLG:
N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]

ChemComp-C2F:
5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID

ChemComp-DOD:
DEUTERATED WATER

Source
  • thermus thermophilus (bacteria)
KeywordsTRANSFERASE / PLP-dependent enzyme / substrate complex / internal aldimine / glycine external aldimine / 5-methyl-tetrahydrofolate

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