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Journal of Bacteriology, May 2004, p. 3266-3269, Vol. 186, No. 10
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.10.3266-3269.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of a Nucleotide-Binding Domain Associated with Neisserial Iron Transport

Gloria H. Y. Lau,1 Ross T. A. MacGillivray,1 and Michael E. P. Murphy1,2*

Department of Biochemistry and Molecular Biology,1 Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada2

Received 22 October 2003/ Accepted 3 February 2004

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-[{gamma}32P]ATP, indicating that FbpC is a functional ATPase that likely combines with FbpB to form a ferric iron transporter.


* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of British Columbia, #300 6174 University Blvd., Vancouver, BC V6T 1Z3, Canada. Phone: (604) 822-8022. Fax: (604) 822-6041. E-mail: memurphy{at}interchange.ubc.ca.


Journal of Bacteriology, May 2004, p. 3266-3269, Vol. 186, No. 10
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.10.3266-3269.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.