Faculty Opinions recommendation of The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a.

2005 ◽  
Author(s):  
Miguel Valvano
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Terminal Domain ◽  
Atp Binding Cassette Transporter ◽  
Domain Protein ◽  
O Antigens

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.

scholarly journals The ATP Hydrolysis Cycle of the Nucleotide-binding Domain of the Mitochondrial ATP-binding Cassette Transporter Mdl1p

2003 ◽  
Vol 278 (29) ◽  
pp. 26862-26869 ◽  
Author(s):  
Eva Janas ◽  
Matthias Hofacker ◽  
Min Chen ◽  
Simone Gompf ◽  
Chris van der Does ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Atp Binding ◽  
Nucleotide Binding Domain ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

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.

Sign in / Sign up

Export Citation Format

Share Document