Format

Send to

Choose Destination
J Bacteriol. 2011 Feb;193(4):887-95. doi: 10.1128/JB.00730-10. Epub 2010 Dec 10.

FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-binding proteins.

Author information

1
Department of Bacteriology, University of Wisconsin, Madison, WI 53706, USA.

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.

PMID:
21148731
PMCID:
PMC3028670
DOI:
10.1128/JB.00730-10
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center