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Structure paper

TitleStructures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100797-100797, Year 2021
Publish dateOct 1, 2020 (structure data deposition date)
AuthorsBrewster, J.L. / Pachl, P. / McKellar, J.L.O. / Selmer, M. / Squire, C.J. / Patrick, W.M.
External linksJ. Biol. Chem. / PubMed:34019879
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-7kb0:
O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7kb1:
Complex of O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima and a key reaction intermediate
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-WBJ:
(2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid

ChemComp-NA:
Unknown entry

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsTRANSFERASE / Thermotoga maritima / methionine biosynthesis / enzyme kinetics / O-acety-L-homoserine aminocarboxypropyltransferase / MetY / active site

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