4B4D
Crystal structure of FAD-containing ferredoxin-NADP reductase from Xanthomonas axonopodis pv. citri
Summary for 4B4D
| Entry DOI | 10.2210/pdb4b4d/pdb |
| Descriptor | FERREDOXIN-NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | XANTHOMONAS AXONOPODIS PV. CITRI STR. 306 |
| Total number of polymer chains | 1 |
| Total formula weight | 30608.81 |
| Authors | Martinez-Julvez, M.,Orellano, E.G.,Tondo, M.L.,Hurtado-Guerrero, R.,Medina, M.,Ceccarelli, E.A.,Sanchez-Azqueta, A. (deposition date: 2012-07-30, release date: 2013-08-21, Last modification date: 2023-12-20) |
| Primary citation | Tondo, M.L.,Hurtado-Guerrero, R.,Sanchez-Azqueta, A.,Ceccarelli, E.A.,Medina, M.,Orellano, E.G.,Martinez-Julvez, M. Crystal Structure of Fad-Containing Ferredoxin- Nadp Reductase from Xanthomonas Axonopodis Pv. Citri Biomed Res Int, 2013:06572-, 2013 Cited by PubMed Abstract: We have solved the structure of ferredoxin-NADP(H) reductase, FPR, from the plant pathogen Xanthomonas axonopodis pv. citri, responsible for citrus canker, at a resolution of 1.5 Å. This structure reveals differences in the mobility of specific loops when compared to other FPRs, probably unrelated to the hydride transfer process, which contributes to explaining the structural and functional divergence between the subclass I FPRs. Interactions of the C-terminus of the enzyme with the phosphoadenosine of the cofactor FAD limit its mobility, thus affecting the entrance of nicotinamide into the active site. This structure opens the possibility of rationally designing drugs against the X. axonopodis pv. citri phytopathogen. PubMed: 23984418DOI: 10.1155/2013/906572 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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