Structural highlights
Publication Abstract from PubMed
The periplasmic protein ApbE was identified through the analysis of several mutants defective in thiamin biosynthesis and 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 that 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 non-functional 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.
FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins.,Boyd JM, Endrizzi JA, Hamilton TL, Christopherson MR, Mulder DW, Downs DM, Peters JW J Bacteriol. 2010 Dec 10. PMID:21148731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyd JM, Endrizzi JA, Hamilton TL, Christopherson MR, Mulder DW, Downs DM, Peters JW. FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins. J Bacteriol. 2010 Dec 10. PMID:21148731 doi:10.1128/JB.00730-10
