scholarly journals The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in BothcisandtransConfigurations

Biochemistry ◽  
2014 ◽  
Vol 53 (46) ◽  
pp. 7148-7159 ◽  
Author(s):  
T. Reid Alderson ◽  
Jin Hae Kim ◽  
Kai Cai ◽  
Ronnie O. Frederick ◽  
Marco Tonelli ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Interdomain Linker

scholarly journals Correction to The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in Both cis and trans Configurations

Biochemistry ◽  
2014 ◽  
Vol 53 (50) ◽  
pp. 7999-7999
Author(s):  
T. Reid Alderson ◽  
Jin Hae Kim ◽  
Kai Cai ◽  
Ronnie O. Frederick ◽  
Marco Tonelli ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Interdomain Linker ◽  
Cis And Trans

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.

scholarly journals Kinetics of the ATP Hydrolysis Cycle of the Nucleotide-binding Domain of Mdl1 Studied by a Novel Site-specific Labeling Technique

2005 ◽  
Vol 281 (9) ◽  
pp. 5694-5701 ◽  
Author(s):  
Chris van der Does ◽  
Chiara Presenti ◽  
Katrin Schulze ◽  
Stephanie Dinkelaker ◽  
Robert Tampé
Keyword(s):  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Site Specific ◽  
Kinetics Of

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 H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB

2005 ◽  
Vol 24 (11) ◽  
pp. 1901-1910 ◽  
Author(s):  
Jelena Zaitseva ◽  
Stefan Jenewein ◽  
Thorsten Jumpertz ◽  
I Barry Holland ◽  
Lutz Schmitt
Keyword(s):  
Abc Transporter ◽  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain

scholarly journals Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

2020 ◽  
Author(s):  
Ljuvica Kolich ◽  
Ya-Ting Chang ◽  
Nicolas Coudray ◽  
Sabrina I. Giacometti ◽  
Mark R. MacRae ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Abc Transporters ◽  
Atp Hydrolysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Regulatory Subunit ◽  
Nucleotide Binding Domain ◽  
Transporter Family ◽  
Bacterial Lipid ◽  
Phospholipid Transport

ABC transporters facilitate the movement of a diverse array of molecules across cellular membranes, using power from ATP hydrolysis. While the overall mechanism of the transport cycle has been characterized in detail for several important members of this transporter family, it is less well understood how the activity of ABC transporters is regulated in the cell post-translationally. Here we report the X-ray crystal structure of MlaFB from E. coli, an ABC nucleotide binding domain (MlaF) in complex with its putative regulatory subunit (MlaB). MlaFB constitutes the cytoplasmic portion of the larger MlaFEDB ABC transporter complex, which drives phospholipid transport across the bacterial envelope and is important for maintaining the integrity of the outer membrane barrier. Our data show that the regulatory subunit MlaB, a STAS domain protein, binds to the nucleotide binding domain and is required for its stability. Our structure also implicates a unique C-terminal tail of the ABC subunit, MlaF, in self-dimerization. Both the C-terminal tail of MlaF and the interaction with MlaB are required for the proper assembly of the MlaFEDB complex and its function in cells. This work leads to a new model for how the activity of an important bacterial lipid transporter may be regulated by small binding proteins, and raises the possibility that similar regulatory mechanisms may exist more broadly across the ABC transporter family, from bacteria to humans.

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