scholarly journals A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells

2021 ◽  
pp. 2003630
Author(s):  
Alexis Voegele ◽  
Mirko Sadi ◽  
Darragh Patrick O'Brien ◽  
Pauline Gehan ◽  
Dorothée Raoux‐Barbot ◽  
...  
Keyword(s):  
Binding Site ◽  
Eukaryotic Cells ◽  
Calmodulin Binding ◽  
High Affinity ◽  
Translocation Domain

scholarly journals Characterization of the Calmodulin-binding Site of Nonerythroid α-Spectrin

1989 ◽  
Vol 264 (10) ◽  
pp. 5826-5830 ◽  
Author(s):  
T L Leto ◽  
S Pleasic ◽  
B G Forget ◽  
E J Benz ◽  
V T Marchesi
Keyword(s):  
Binding Site ◽  
Calmodulin Binding

scholarly journals Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa

2006 ◽  
Vol 400 (3) ◽  
pp. 385-392 ◽  
Author(s):  
Erdeni Bai ◽  
Federico I. Rosell ◽  
Bao Lige ◽  
Marcia R. Mauk ◽  
Barbara Lelj-Garolla ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Ions ◽  
Binding Site ◽  
Metal Ion ◽  
Association Constants ◽  
Ion Binding ◽  
Ferric Uptake Regulator ◽  
Metal Ion Binding ◽  
Dimerization Domain ◽  
High Affinity

The functional properties of the recombinant C-terminal dimerization domain of the Pseudomonas aeruginosa Fur (ferric uptake regulator) protein expressed in and purified from Escherichia coli have been evaluated. Sedimentation velocity measurements demonstrate that this domain is dimeric, and the UV CD spectrum is consistent with a secondary structure similar to that observed for the corresponding region of the crystallographically characterized wild-type protein. The thermal stability of the domain as determined by CD spectroscopy decreases significantly as pH is increased and increases significantly as metal ions are added. Potentiometric titrations (pH 6.5) establish that the domain possesses a high-affinity and a low-affinity binding site for metal ions. The high-affinity (sensory) binding site demonstrates association constants (KA) of 10(±7)×106, 5.7(±3)×106, 2.0(±2)×106 and 2.0(±3)×104 M−1 for Ni2+, Zn2+, Co2+ and Mn2+ respectively, while the low-affinity (structural) site exhibits association constants of 1.3(±2)×106, 3.2(±2)×104, 1.76(±1)×105 and 1.5(±2)×103 M−1 respectively for the same metal ions (pH 6.5, 300 mM NaCl, 25 °C). The stability of metal ion binding to the sensory site follows the Irving–Williams order, while metal ion binding to the partial sensory site present in the domain does not. Fluorescence experiments indicate that the quenching resulting from binding of Co2+ is reversed by subsequent titration with Zn2+. We conclude that the domain is a reasonable model for many properties of the full-length protein and is amenable to some analyses that the limited solubility of the full-length protein prevents.

Characterization of a Specific, High Affinity [3H]Arginine8Vasopressin-Binding Site on Liver Microsomes from Different Strains of Rat and the Role of Magnesium*

Endocrinology ◽  
1986 ◽  
Vol 118 (3) ◽  
pp. 990-998 ◽  
Author(s):  
VENKAT GOPALAKRISHNAN ◽  
CHRIS R. TRIGGLE ◽  
PRAKASH V. SULAKHE ◽  
J. ROBERT McNEILL
Keyword(s):  
Binding Site ◽  
Liver Microsomes ◽  
High Affinity ◽  
Different Strains

Iron-Blocking the High-Affinity Mn-Binding Site in Photosystem II Facilitates Identification of the Type of Hydrogen Bond Participating in Proton-Coupled Electron Transport via YZ•†

Biochemistry ◽  
2005 ◽  
Vol 44 (28) ◽  
pp. 9746-9757 ◽  
Author(s):  
Boris K. Semin ◽  
Elena R. Lovyagina ◽  
Kirill N. Timofeev ◽  
Ilya I. Ivanov ◽  
Andrei B. Rubin ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Electron Transport ◽  
Photosystem Ii ◽  
Binding Site ◽  
High Affinity
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