Mutations in the Nucleotide Binding Domain of the α Subunits of the F1-ATPase from ThermophilicBacillusPS3 That Affect Cross-Talk between Nucleotide Binding Sites†

Biochemistry ◽  
1998 ◽  
Vol 37 (4) ◽  
pp. 1007-1014 ◽  
Author(s):  
Neil B. Grodsky ◽  
Chao Dou ◽  
William S. Allison
Keyword(s):  
Cross Talk ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
F1 Atpase ◽  
Nucleotide Binding Sites ◽  
Α Subunits

scholarly journals Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy

2011 ◽  
Vol 32 (2) ◽  
pp. 531-535 ◽  
Author(s):  
Nam-Kung Jun ◽  
Joon-Hyung Sohn ◽  
Byung-Il Yeh ◽  
Jong-Whan Choi ◽  
Hyun-Won Kim
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites

SPECIFICITY OF REGULATORY NUCLEOTIDE BINDING SITES OF MITOCHONDRIAL F1-ATPase

1981 ◽  
Vol 9 (2) ◽  
pp. 356P-356P
Author(s):  
A. Di Pietro ◽  
H. Baubichon ◽  
C. Godinot ◽  
D. C. Gautheron
Keyword(s):  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites

scholarly journals Unravelling the Interaction of Piperlongumine with the Nucleotide-Binding Domain of HSP70: A Spectroscopic and In Silico Study

2021 ◽  
Vol 14 (12) ◽  
pp. 1298
Author(s):  
Ana Paula Ribeiro Povinelli ◽  
Gabriel Zazeri ◽  
Alan M. Jones ◽  
Marinônio Lopes Cornélio
Keyword(s):  
Binding Sites ◽  
Protein Secondary Structure ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Time Resolved ◽  
In Silico Study ◽  
Molecular Mode ◽  
Steady State Fluorescence Spectroscopy ◽  
Thermal Stability Of

Piperlongumine (PPL) is an alkaloid extracted from several pepper species that exhibits anti-inflammatory and anti-carcinogenic properties. Nevertheless, the molecular mode of action of PPL that confers such powerful pharmacological properties remains unknown. From this perspective, spectroscopic methods aided by computational modeling were employed to characterize the interaction between PPL and nucleotide-binding domain of heat shock protein 70 (NBD/HSP70), which is involved in the pathogenesis of several diseases. Steady-state fluorescence spectroscopy along with time-resolved fluorescence revealed the complex formation based on a static quenching mechanism. Van’t Hoff analyses showed that the binding of PPL toward NBD is driven by equivalent contributions of entropic and enthalpic factors. Furthermore, IDF and Scatchard methods applied to fluorescence intensities determined two cooperative binding sites with Kb of (6.3 ± 0.2) × 104 M−1. Circular dichroism determined the thermal stability of the NBD domain and showed that PPL caused minor changes in the protein secondary structure. Computational simulations elucidated the microenvironment of these interactions, showing that the binding sites are composed mainly of polar amino acids and the predominant interaction of PPL with NBD is Van der Waals in nature.

Temperature-induced states of isolated F1-ATPase affect catalysis, enzyme conformation and high-affinity nucleotide binding sites

1989 ◽  
Vol 976 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Alessandra Baracca ◽  
Evzen Amler ◽  
Giancarlo Solaini ◽  
Giovanna Parenti Castelli ◽  
Giorgio Lenaz ◽  
...  
Keyword(s):  
Binding Sites ◽  
Nucleotide Binding ◽  
F1 Atpase ◽  
Nucleotide Binding Sites ◽  
High Affinity

scholarly journals Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5

2008 ◽  
Vol 283 (50) ◽  
pp. 35010-35022 ◽  
Author(s):  
Zuben E. Sauna ◽  
Sherry Supernavage Bohn ◽  
Robert Rutledge ◽  
Michael P. Dougherty ◽  
Susan Cronin ◽  
...  
Keyword(s):  
Cross Talk ◽  
Transmembrane Helix ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Multidrug Transporter ◽  
Nucleotide Binding Domain ◽  
Terminal Nucleotide
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