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TitleNew insights into the function and molecular mechanisms of Ferredoxin-NADP + reductase from Brucella ovis.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 762, Page 110204-110204, Year 2024
Publish dateSep 29, 2024 (structure data deposition date)
AuthorsMoreno, A. / Quereda-Moraleda, I. / Lozano-Vallhonrat, C. / Bunuel-Escudero, M. / Botha, S. / Kupitz, C. / Lisova, S. / Sierra, R. / Mariani, V. / Schleissner, P. ...Moreno, A. / Quereda-Moraleda, I. / Lozano-Vallhonrat, C. / Bunuel-Escudero, M. / Botha, S. / Kupitz, C. / Lisova, S. / Sierra, R. / Mariani, V. / Schleissner, P. / Gee, L.B. / Dorner, K. / Schmidt, C. / Han, H. / Kloos, M. / Smyth, P. / Valerio, J. / Schulz, J. / de Wijn, R. / Melo, D.V.M. / Round, A. / Trost, F. / Sobolev, E. / Juncheng, E. / Sikorski, M. / Bean, R. / Martinez-Julvez, M. / Martin-Garcia, J.M. / Medina, M.
External linksArch. Biochem. Biophys. / PubMed:39522858
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-9gxb:
Room temperature structure of FAD-containing ferrodoxin-NADP reductase from Brucella ovis at EuXFEL
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-9gxc:
Room temperature structure of FAD-containing ferrodoxin-NADP reductase from Brucella ovis at LCLS
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

Source
  • brucella ovis atcc 25840 (bacteria)
KeywordsOXIDOREDUCTASE / ferredoxin-NADP+ reductase / room temperature X-ray diffraction / electron transfer / oxidative damage protection / serial femtosecond crystallography / XFEL / microcrystals.

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