2BMW
Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr, Leu 263 Replaced By Pro, Arg 264 Replaced By Pro and Gly 265 Replaced by Pro (T155G-A160T-L263P-R264P-G265P)
Summary for 2BMW
| Entry DOI | 10.2210/pdb2bmw/pdb |
| Related | 2BMV |
| Descriptor | FERREDOXIN--NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, flavoprotein, nadp, fad, fnr, reductase reductase, phycobilisome, thylakoid |
| Biological source | ANABAENA SP. (CYANOBACTERIA) |
| Cellular location | Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P21890 |
| Total number of polymer chains | 1 |
| Total formula weight | 35004.39 |
| Authors | Martinez-Julvez, M.,Hermoso, J.A.,Perez-Dorado, I.,Medina, M.,Tejero, J.,Gomez-Moreno, C. (deposition date: 2005-03-16, release date: 2006-06-22, Last modification date: 2023-12-13) |
| Primary citation | Peregrina, J.R.,Herguedas, B.,Hermoso, J.A.,Martinez-Julvez, M.,Medina, M. Protein Motifs Involved in Coenzyme Interaction and Enzymatic Efficiency in Anabaena Ferredoxin-Nadp+ Reductase. Biochemistry, 48:3109-, 2009 Cited by PubMed Abstract: Ferredoxin-NADP+ reductases (FNRs) must determine the coenzyme specificity and allow the transient encounter between N5 of its flavin cofactor and C4 of the coenzyme nicotinamide for efficient hydride transfer. Combined site-directed replacements in different putative determinants of the FNR coenzyme specificity were simultaneously produced. The resulting variants were structurally and functionally analyzed for their binding and hydride transfer abilities to the FNR physiological coenzyme NADP+/H, as well as to NAD+/H. The previously studied Y303S mutation is the only one that significantly enhances specificity for NAD+. Combination of mutations from the pyrophosphate or 2'-phosphate regions, even including Y303S, does not improve activity with NAD+, despite structures of these FNRs show how particular coenzyme-binding regions resembled motifs found in NAD+/H-dependent enzymes of the FNR family. Therefore, the "rational approach" did not succeed well, and coenzyme specificity redesign in the FNR family will be more complex than that anticipated in other NADP+/NAD+ families. PubMed: 19219975DOI: 10.1021/BI802077C PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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