Sequence Requirements of the ATP-Binding Site within the C-Terminal Nucleotide-Binding Domain of Mouse P-Glycoprotein:  Structure−Activity Relationships for Flavonoid Binding†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10382-10391 ◽  
Author(s):  
Heidi de Wet ◽  
David B. McIntosh ◽  
Gwenaëlle Conseil ◽  
Hélène Baubichon-Cortay ◽  
Tino Krell ◽  
...  
Keyword(s):  
Binding Site ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Atp Binding Site ◽  
Structure Activity ◽  
P Glycoprotein ◽  
Glycoprotein Structure ◽  
Sequence Requirements

scholarly journals Identification of the Magnesium-binding Domain of the High-affinity ATP-binding Site of theBacillus subtilisandEscherichia coliSecA Protein

1995 ◽  
Vol 270 (32) ◽  
pp. 18975-18982 ◽  
Author(s):  
Jeroen P. W. van der Wolk ◽  
Michael Klose ◽  
Janny G. de Wit ◽  
Tanneke den Blaauwen ◽  
Roland Freudl ◽  
...  
Keyword(s):  
Binding Site ◽  
Binding Domain ◽  
Atp Binding ◽  
Atp Binding Site ◽  
High Affinity ◽  
Magnesium Binding

Allosteric effects of ATP binding on the nucleotide-binding domain of a heterodimeric ATP-binding cassette transporter

2016 ◽  
Vol 8 (11) ◽  
pp. 1158-1169
Author(s):  
Xianchao Pan ◽  
Qiaoxia Zhang ◽  
Sujun Qu ◽  
Shuheng Huang ◽  
Huicong Wang ◽  
...  
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

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

Trypanosoma cruzi: Sequence of the ATP-Binding Site of a P-Glycoprotein Gene

1994 ◽  
Vol 79 (1) ◽  
pp. 63-67 ◽  
Author(s):  
B. Dallagiovanna ◽  
S. Castanys ◽  
F. Gamarro
Keyword(s):  
Trypanosoma Cruzi ◽  
Binding Site ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Glycoprotein Gene ◽  
P Glycoprotein

scholarly journals Complete Dissociation of an ATP-Binding Cassette Nucleotide-Binding Domain during the Hydrolysis Cycle

2012 ◽  
Vol 102 (3) ◽  
pp. 266a
Author(s):  
Maria E. Zoghbi ◽  
Srinivasan Krishnan ◽  
Guillermo A. Altenberg
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Complete Dissociation ◽  
Atp Binding Cassette

scholarly journals The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP

2004 ◽  
Vol 377 (1) ◽  
pp. 95-105 ◽  
Author(s):  
Juha OKKERI ◽  
Liisa LAAKKONEN ◽  
Tuomas HALTIA
Keyword(s):  
Escherichia Coli ◽  
Sarcoplasmic Reticulum ◽  
Binding Site ◽  
Molecular Model ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Disease Mutations ◽  
Disease Protein ◽  
P Type

In P-type ATPases, the nucleotide-binding (N) domain is located in the middle of the sequence which folds into the phosphorylation (P) domain. The N domain of ZntA, a Zn2+-translocating P-type ATPase from Escherichia coli, is approx. 13% identical with the N domain of sarcoplasmic reticulum Ca2+-ATPase. None of the Ca2+-ATPase residues involved in binding of ATP are found in ZntA. However, the sequence G503SGIEAQV in the N domain of ZntA resembles the motif GxGxxG, which forms part of the ATP-binding site in protein kinases. This motif is also found in Wilson disease protein where several disease mutations cluster in it. In the present work, we have made a set of disease mutation analogues, including the mutants G503S (Gly503→Ser), G505R and A508F of ZntA. At low [ATP], these mutant ATPases are poorly phosphorylated. The phosphorylation defect of the mutants G503S and G505R can, however, be partially (G503S) or fully (G505R) compensated for by using a higher [ATP], suggesting that these mutations lower the affinity for ATP. In all three mutant ATPases, phosphorylation by Pi has become less sensitive to the presence of ATP, also consistent with the proposal that the Gly503 motif plays a role in ATP binding. In order to test this hypothesis, we have modelled the N domain of ZntA using the sarcoplasmic reticulum Ca2+-ATPase structure as a template. In the model, the Gly503 motif, as well as the residues Glu470 and His475, are located in the proximity of the ATP-binding site. In conclusion, the mutagenesis data and the molecular model are consistent with the idea that the two loops carrying the residues Glu470, His475, Gly503 and Gly505 play a role in ATP binding and activation.

scholarly journals ATP Binding by Monarch-1/NLRP12 Is Critical for Its Inhibitory Function

2007 ◽  
Vol 28 (5) ◽  
pp. 1841-1850 ◽  
Author(s):  
Zhengmao Ye ◽  
John D. Lich ◽  
Chris B. Moore ◽  
Joseph A. Duncan ◽  
Kristi L. Williams ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Interleukin 1 ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Hairpin Rna ◽  
Inhibitory Function ◽  
Cytokines And Chemokines ◽  
Hydrolysis Activity

ABSTRACT The recently discovered nucleotide binding domain-leucine rich repeat (NLR) gene family is conserved from plants to mammals, and several members are associated with human autoinflammatory or immunodeficiency disorders. This family is defined by a central nucleotide binding domain that contains the highly conserved Walker A and Walker B motifs. Although the nucleotide binding domain is a defining feature of this family, it has not been extensively studied in its purified form. In this report, we show that purified Monarch-1/NLRP12, an NLR protein that negatively regulates NF-κB signaling, specifically binds ATP and exhibits ATP hydrolysis activity. Intact Walker A/B motifs are required for this activity. These motifs are also required for Monarch-1 to undergo self-oligomerization, Toll-like receptor- or CD40L-activated association with NF-κB-inducing kinase (NIK) and interleukin-1 receptor-associated kinase 1 (IRAK-1), degradation of NIK, and inhibition of IRAK-1 phosphorylation. The stable expression of a Walker A/B mutant in THP-1 monocytes results in increased production of proinflammatory cytokines and chemokines to an extent comparable to that in cells in which Monarch-1 is silenced via short hairpin RNA. The results of this study are consistent with a model wherein ATP binding regulates the anti-inflammatory activity of Monarch-1.

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