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TitleResidue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme.
Journal, issue, pagesBiochemistry, Vol. 48, Page 3138-3145, Year 2009
Publish dateFeb 17, 2009 (structure data deposition date)
AuthorsMera, P.E. / St Maurice, M. / Rayment, I. / Escalante-Semerena, J.C.
External linksBiochemistry / PubMed:19236001
MethodsX-ray diffraction
Resolution1.17 - 1.48 Å
Structure data

PDB-3gah:
Structure of a F112H variant PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP
Method: X-RAY DIFFRACTION / Resolution: 1.17 Å

PDB-3gai:
Structure of a F112A variant PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

PDB-3gaj:
Structure of a C-terminal deletion variant of a PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri complexed with cobalamin and ATP
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-B12:
COBALAMIN

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • lactobacillus reuteri (bacteria)
KeywordsTRANSFERASE

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