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

2004 ◽  
Vol 186 (10) ◽  
pp. 3266-3269 ◽  
Author(s):  
Gloria H. Y. Lau ◽  
Ross T. A. MacGillivray ◽  
Michael E. P. Murphy

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-[γ32P]ATP, indicating that FbpC is a functional ATPase that likely combines with FbpB to form a ferric iron transporter.

2016 ◽  
Vol 8 (11) ◽  
pp. 1158-1169
Author(s):  
Xianchao Pan ◽  
Qiaoxia Zhang ◽  
Sujun Qu ◽  
Shuheng Huang ◽  
Huicong Wang ◽  
...  

The dimerization of asymmetric NBDs was exclusively triggered by ATP bound at the consensus ATPase site.


2012 ◽  
Vol 102 (3) ◽  
pp. 330a
Author(s):  
Maria J. Marques Carvalho ◽  
Ricardo S. Vieira Pires ◽  
Guillaume Gabant ◽  
Martine Cadene ◽  
João H. Morais Cabral

1997 ◽  
Vol 7 (16) ◽  
pp. 2109-2114 ◽  
Author(s):  
Joseph A. Maddry ◽  
Conrad Kussner ◽  
Jackie W. Truss ◽  
Shri Niwas ◽  
E. Lucile White ◽  
...  

2003 ◽  
Vol 278 (29) ◽  
pp. 26862-26869 ◽  
Author(s):  
Eva Janas ◽  
Matthias Hofacker ◽  
Min Chen ◽  
Simone Gompf ◽  
Chris van der Does ◽  
...  

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