scholarly journals Selective Inhibition of DNA Replicase Assembly by a Non-natural Nucleotide: Exploiting the Structural Diversity of ATP-Binding Sites

2009 ◽  
Vol 5 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Kevin Eng ◽  
Sarah K. Scouten-Ponticelli ◽  
Mark Sutton ◽  
Anthony Berdis
Keyword(s):  
Binding Sites ◽  
Structural Diversity ◽  
Selective Inhibition ◽  
Atp Binding ◽  
Dna Replicase

Urea-induced transformation of native estrogen receptor and evidence for separate DNA- and ATP-binding sites

1986 ◽  
Vol 139 (3) ◽  
pp. 1250-1255 ◽  
Author(s):  
T. William Hutchens ◽  
Chee Ming Li ◽  
Paige K. Besch
Keyword(s):  
Estrogen Receptor ◽  
Binding Sites ◽  
Atp Binding

Distribution of [3H]α,β-methylene ATP binding sites in rat brain and spinal cord

Neuroreport ◽  
1994 ◽  
Vol 5 (13) ◽  
pp. 1601-1604 ◽  
Author(s):  
Xuenong Bo ◽  
Geoffrey Burnstock
Keyword(s):  
Spinal Cord ◽  
Rat Brain ◽  
Binding Sites ◽  
Atp Binding ◽  
Brain And Spinal Cord

Mapping multiple potential ATP binding sites on the matrix side of the bovine ADP/ATP carrier by the combined use of MD simulation and docking

2011 ◽  
Vol 18 (6) ◽  
pp. 2377-2386 ◽  
Author(s):  
Daniele Di Marino ◽  
Francesco Oteri ◽  
Blasco Morozzo della Rocca ◽  
Ilda D’Annessa ◽  
Mattia Falconi
Keyword(s):  
Binding Sites ◽  
Md Simulation ◽  
Atp Binding ◽  
Combined Use ◽  
The Matrix

scholarly journals A novel sequence-based prediction method for ATP-binding sites using fusion of SMOTE algorithm and random forests classifier

2020 ◽  
Vol 34 (1) ◽  
pp. 1336-1346
Author(s):  
Jiazhi Song ◽  
Guixia Liu ◽  
Chuyi Song ◽  
Jingqing Jiang
Keyword(s):  
Random Forests ◽  
Binding Sites ◽  
Prediction Method ◽  
Atp Binding

Evidence for three atp binding sites in the (Na+ + K+)-ATPase

1979 ◽  
Vol 10 (9) ◽  
pp. xv
Author(s):  
Hermann Koepsell
Keyword(s):  
Binding Sites ◽  
Atp Binding

scholarly journals One Intact Transmembrane Substrate Binding Site Is Sufficient for the Function of the Homodimeric Type I ATP-Binding Cassette Importer for Positively Charged Amino Acids Art(MP) 2 of Geobacillus stearothermophilus

2018 ◽  
Vol 200 (12) ◽  
Author(s):  
Johanna Heuveling ◽  
Heidi Landmesser ◽  
Erwin Schneider
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Substrate Binding ◽  
Binding Pocket ◽  
Atp Binding ◽  
Content Type ◽  
Charged Amino Acids ◽  
Substrate Binding Sites ◽  
Positively Charged ◽  
Atp Binding Cassette

ABSTRACT ATP-binding cassette (ABC) transport systems comprise two transmembrane domains/subunits that form a translocation path and two nucleotide-binding domains/subunits that bind and hydrolyze ATP. Prokaryotic canonical ABC import systems require an extracellular substrate-binding protein for function. Knowledge of substrate-binding sites within the transmembrane subunits is scarce. Recent crystal structures of the ABC importer Art(QN) 2 for positively charged amino acids of Thermoanerobacter tengcongensis revealed the presence of one substrate molecule in a defined binding pocket in each of the transmembrane subunits, ArtQ (J. Yu, J. Ge, J. Heuveling, E. Schneider, and M. Yang, Proc Natl Acad Sci U S A 112:5243–5248, 2015, https://doi.org/10.1073/pnas.1415037112 ). This finding raised the question of whether both sites must be loaded with substrate prior to initiation of the transport cycle. To address this matter, we first explored the role of key residues that form the binding pocket in the closely related Art(MP) 2 transporter of Geobacillus stearothermophilus , by monitoring consequences of mutations in ArtM on ATPase and transport activity at the level of purified proteins embedded in liposomes. Our results emphasize that two negatively charged residues (E153 and D160) are crucial for wild-type function. Furthermore, the variant Art[M(L67D)P] 2 exhibited strongly impaired activities, which is why it was considered for construction of a hybrid complex containing one intact and one impaired substrate-binding site. Activity assays clearly revealed that one intact binding site was sufficient for function. To our knowledge, our study provides the first biochemical evidence on transmembrane substrate-binding sites of an ABC importer. IMPORTANCE Canonical prokaryotic ATP-binding cassette importers mediate the uptake of a large variety of chemicals, including nutrients, osmoprotectants, growth factors, and trace elements. Some also play a role in bacterial pathogenesis, which is why full understanding of their mode of action is of the utmost importance. One of the unsolved problems refers to the chemical nature and number of substrate binding sites formed by the transmembrane subunits. Here, we report that a hybrid amino acid transporter of G. stearothermophilus , encompassing one intact and one impaired transmembrane binding site, is fully competent in transport, suggesting that the binding of one substrate molecule is sufficient to trigger the translocation process.

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