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TitleMutational and structural studies of ( beta alpha ) 8 -barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism.
Journal, issue, pagesProtein Sci., Vol. 33, Page e5018-e5018, Year 2024
Publish dateOct 2, 2023 (structure data deposition date)
AuthorsGehl, M. / Demmer, U. / Ermler, U. / Shima, S.
External linksProtein Sci. / PubMed:38747406
MethodsX-ray diffraction
Resolution1.75 - 2 Å
Structure data

PDB-8qpj:
FAD-independent Methylene-Tetrahydrofolate Reductase Mutant E9Q from Mycobacterium hassiacum
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-8qpl:
F420-Dependent Methylene-Tetrahydromethanopterin Reductase with F420 from Methanocaldococcus jannaschii
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-8qpm:
Structure of methylene-tetrahydromethanopterin reductase from Methanocaldococcus jannaschii
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-8qq8:
Crystal Structure of F420-dependent Methylene-Tetrahydromethanopterin Reductase Mutant E6Q from Methanocaldococcus Jannaschii
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-F42:
COENZYME F420

Source
  • mycolicibacterium hassiacum (bacteria)
  • methanocaldococcus jannaschii (archaea)
KeywordsOXIDOREDUCTASE / Methylenetetrahydrofolate reductase / methylene-tetrahydrofolate reductase / F420-dependent methylene-tetrahydromethanopterin reductase / F420 / methylene-tetrahydropterin reductase

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