9GXC
Room temperature structure of FAD-containing ferrodoxin-NADP reductase from Brucella ovis at LCLS
Summary for 9GXC
| Entry DOI | 10.2210/pdb9gxc/pdb |
| Descriptor | ferredoxin--NADP(+) reductase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | ferredoxin-nadp+ reductase, room temperature x-ray diffraction, electron transfer, oxidative damage protection, serial femtosecond crystallography, xfel, microcrystals., oxidoreductase |
| Biological source | Brucella ovis ATCC 25840 |
| Total number of polymer chains | 1 |
| Total formula weight | 31490.14 |
| Authors | Martinez-Julvez, M.,Martin-Garcia, J.M.,Medina, M. (deposition date: 2024-09-29, release date: 2024-11-27) |
| Primary citation | 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. New insights into the function and molecular mechanisms of Ferredoxin-NADP + reductase from Brucella ovis. Arch.Biochem.Biophys., 762:110204-110204, 2024 Cited by PubMed Abstract: Bacterial ferredoxin(flavodoxin)-NADP reductases (FPR) primarily catalyze the transfer of reducing equivalents from NADPH to ferredoxin (or flavodoxin) to provide low potential reducing equivalents for the oxidoreductive metabolism. In addition, they can be implicated in regulating reactive oxygen species levels. Here we assess the functionality of FPR from B. ovis to understand its potential roles in the bacteria physiology. We prove that this FPR is active with the endogenous [2Fe-2S] Fdx ferredoxin, exhibiting a K in the low micromolar range. At the molecular level, this study provides with the first structures of an FPR at room temperature obtained by serial femtosecond crystallography, envisaging increase in flexibility at both the adenine nucleotide moiety of FAD and the C-terminal tail. The produced microcrystals are in addition suitable for future mix-and-inject time-resolved studies with the NADP/H coenzyme either at synchrotrons or XFELs. Furthermore, the study also predicts the ability of FPR to simultaneously interact with Fdx and NADP/H. PubMed: 39522858DOI: 10.1016/j.abb.2024.110204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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