PMID:15126492
| Citation |
Lau, GH, MacGillivray, RT and Murphy, ME (2004) Characterization of a nucleotide-binding domain associated with neisserial iron transport. J. Bacteriol. 186:3266-9 |
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| Abstract |
The fbpABC operon in Neisseria gonorrhoeae encodes an ATP-binding cassette transporter required for iron uptake from the host ferric binding proteins. The gene for the nucleotide-binding domain (fbpC) expressed in Escherichia coli has intrinsic ATPase activity (0.5 mmol/min/mg) uncoupled from the iron transport process. The FbpC E164D mutant is found to have a 10-fold reduction in specific activity. FbpC is covalently modified by 8-azido-[gamma32P]ATP, indicating that FbpC is a functional ATPase that likely combines with FbpB to form a ferric iron transporter. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Azides/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Cation Transport Proteins/chemistry; Cation Transport Proteins/metabolism; Ion Transport; Molecular Sequence Data; Mutagenesis, Site-Directed; Neisseria gonorrhoeae/metabolism; Recombinant Proteins/metabolism; Structure-Activity Relationship |
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