Characterization of a nucleotide-binding domain associated with neisserial iron transport.
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ABSTRACT:
SUBMITTER: Lau GH
PROVIDER: S-EPMC400613 | biostudies-literature | 2004 May
REPOSITORIES: biostudies-literature
Publications
Characterization of a nucleotide-binding domain associated with neisserial iron transport.
Lau Gloria H Y GH MacGillivray Ross T A RT Murphy Michael E P ME
Journal of bacteriology 20040501 10
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 ...[more]
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