scholarly journals Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase

2013 ◽  
Vol 41 (20) ◽  
pp. 9557-9569 ◽  
Author(s):  
Nikhil Jain ◽  
Neha Vithani ◽  
Abu Rafay ◽  
Balaji Prakash
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Ribosome Binding ◽  
Identification And Characterization

scholarly journals Structural and Biochemical Characterization of a Cyclic Nucleotide Binding Domain from the EAG Family

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

Inhibition of the her2 tyrosine kinase and characterization of a hydrophobic site near the nucleotide binding domain

1997 ◽  
Vol 7 (16) ◽  
pp. 2109-2114 ◽  
Author(s):  
Joseph A. Maddry ◽  
Conrad Kussner ◽  
Jackie W. Truss ◽  
Shri Niwas ◽  
E. Lucile White ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Hydrophobic Site

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
Keyword(s):  
Iron Uptake ◽  
Iron Transport ◽  
Ferric Iron ◽  
Specific Activity ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Atp Binding Cassette Transporter ◽  
Fold Reduction

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.

scholarly journals Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Fabia Furtmann ◽  
Nicola Porta ◽  
Dai Tri Hoang ◽  
Jens Reiners ◽  
Julia Schumacher ◽  
...  
Keyword(s):  
Streptococcus Agalactiae ◽  
Bacterial Infections ◽  
Nucleotide Binding ◽  
Resistance Mechanisms ◽  
Binding Domain ◽  
Binding Modes ◽  
Human Pathogens ◽  
Nucleotide Binding Domain ◽  
Transporter Family

Abstract Treatment of bacterial infections is a great challenge of our era due to the various resistance mechanisms against antibiotics. Antimicrobial peptides are considered to be potential novel compound as antibiotic treatment. However, some bacteria, especially many human pathogens, are inherently resistant to these compounds, due to the expression of BceAB-type ABC transporters. This rather new transporter family is not very well studied. Here, we report the first full characterization of the nucleotide binding domain of a BceAB type transporter from Streptococcus agalactiae, namely SaNsrF of the transporter SaNsrFP, which confers resistance against nisin and gallidermin. We determined the NTP hydrolysis kinetics and used molecular modeling and simulations in combination with small angle X-ray scattering to obtain structural models of the SaNsrF monomer and dimer. The fact that the SaNsrFH202A variant displayed no ATPase activity was rationalized in terms of changes of the structural dynamics of the dimeric interface. Kinetic data show a clear preference for ATP as a substrate, and the prediction of binding modes allowed us to explain this selectivity over other NTPs.

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