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Structure paper

TitleThe trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes.
Journal, issue, pagesSci Rep, Vol. 7, Page 404-404, Year 2017
Publish dateNov 17, 2015 (structure data deposition date)
AuthorsSerrano, A. / Sebastian, M. / Arilla-Luna, S. / Baquedano, S. / Herguedas, B. / Velazquez-Campoy, A. / Martinez-Julvez, M. / Medina, M.
External linksSci Rep / PubMed:28341845
MethodsX-ray diffraction
Resolution2.45 - 2.52 Å
Structure data

PDB-5fnz:
F206W mutant of FAD synthetase from Corynebacterium ammoniagenes
Method: X-RAY DIFFRACTION / Resolution: 2.52 Å

PDB-5fo0:
D298E mutant of FAD synthetase from Corynebacterium ammoniagenes
Method: X-RAY DIFFRACTION / Resolution: 2.51 Å

PDB-5fo1:
E301A mutant of FAD synthetase from Corynebacterium ammoniagenes
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-PPV:
PYROPHOSPHATE

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • corynebacterium ammoniagenes (bacteria)
KeywordsTRANSFERASE / RIBOFLAVIN KINASE / NUCLEOTIDE-BINDING / ATP- BINDING / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE

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