3PND
FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins
Summary for 3PND
| Entry DOI | 10.2210/pdb3pnd/pdb |
| Related | 1VRM 2O18 |
| Descriptor | Thiamine biosynthesis lipoprotein ApbE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | apbe, fad, flavoprotein, oxidoreductase, fad binding domain, t-fold, protein binding |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Cellular location | Cell membrane; Lipid-anchor (Potential): P41780 |
| Total number of polymer chains | 4 |
| Total formula weight | 155312.08 |
| Authors | Boyd, J.M.,Endrizzi, J.A.,Hamilton, T.L.,Christopherson, M.R.,Mulder, D.W.,Downs, D.M.,Peters, J.W. (deposition date: 2010-11-18, release date: 2011-01-05, Last modification date: 2023-09-06) |
| Primary citation | Boyd, J.M.,Endrizzi, J.A.,Hamilton, T.L.,Christopherson, M.R.,Mulder, D.W.,Downs, D.M.,Peters, J.W. FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-binding proteins. J.Bacteriol., 193:887-895, 2011 Cited by PubMed Abstract: The periplasmic protein ApbE was identified through the analysis of several mutants defective in thiamine biosynthesis and was implicated as having a role in iron-sulfur cluster biosynthesis or repair. While mutations in apbE cause decreased activity of several iron-sulfur enzymes in vivo, the specific role of ApbE remains unknown. Members of the AbpE family include NosX and RnfF, which have been implicated in oxidation-reduction associated with nitrous oxide and nitrogen metabolism, respectively. In this work, we show that ApbE binds one FAD molecule per monomeric unit. The structure of ApbE in the presence of bound FAD reveals a new FAD-binding motif. Protein variants that are nonfunctional in vivo were generated by random and targeted mutagenesis. Each variant was substituted in the environment of the FAD and analyzed for FAD binding after reconstitution. The variant that altered a key tyrosine residue involved in FAD binding prevented reconstitution of the protein. PubMed: 21148731DOI: 10.1128/JB.00730-10 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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