scholarly journals Functional hot spots in human ATP-binding cassette transporter nucleotide binding domains

2010 ◽  
Vol 19 (11) ◽  
pp. 2110-2121 ◽  
Author(s):  
Libusha Kelly ◽  
Hisayo Fukushima ◽  
Rachel Karchin ◽  
Jason M. Gow ◽  
Leslie W. Chinn ◽  
...  
Keyword(s):  
Hot Spots ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Binding Domains ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals Interaction between ATP, oleandomycin and the OleB ATP-binding cassette transporter of Streptomyces antibioticus involved in oleandomycin secretion

1997 ◽  
Vol 321 (1) ◽  
pp. 139-144 ◽  
Author(s):  
André BUCHE ◽  
Carmen MÉNDEZ ◽  
José A. SALAS
Keyword(s):  
Fusion Protein ◽  
Nucleotide Binding ◽  
Intrinsic Fluorescence ◽  
Atp Binding ◽  
Hydrophobic Membrane ◽  
Streptomyces Antibioticus ◽  
Binding Domains ◽  
Atp Binding Cassette Transporter ◽  
Guanidine Chloride ◽  
Atp Binding Cassette

The OleB protein of Streptomyces antibioticus, oleandomycin (OM) producer, constitutes an ATP-binding cassette transporter containing two nucleotide-binding domains and is involved in OM resistance and its secretion in this producer strain. We have characterized some properties of the first nucleotide-binding domain of OleB using an overexpressed fusion protein (MBP–OleB´) between a maltose-binding protein (MBP) and the first half of OleB (OleB´). Extrinsic fluorescence of the base-modified fluorescent nucleotide analogue 1,N6-ethenoadenosine 5´-triphosphate (εATP) and 2´(3´)-o-(2,4,6-trinitrophenyl)adenosine-5´-triphosphate was determined in the presence of MBP and the fusion protein MBP–OleB´, and it was found that εATP binds to MBP–OleB´ with a stoichiometry of 0.9. Measurements of the intrinsic fluorescence of the MBP–OleB´ fusion protein indicated that ATP induces a decrease in the accessibility of the MBP–OleB´ tryptophans to acrylamide, an indication of a folding effect. This conclusion was confirmed by the fact that ATP also induces considerable stabilization against guanidine chloride denaturation of MBP–OleB´. Two effects were found to be associated with the presence of Mg2+ ions: (1) an increase in the quenching of MBP–OleB´ intrinsic fluorescence by ATP; and (2) an increase in the accessibility of MBP–OleB´ tryptophans to acrylamide. Significant changes in the intrinsic fluorescence of the fusion protein were also observed in the presence of OM, demostrating the existence of interaction between the transporter and the antibiotic in the absence of any hydrophobic membrane component.

scholarly journals Association/Dissociation of the Nucleotide-binding Domains of the ATP-binding Cassette Protein MsbA Measured during Continuous Hydrolysis

2013 ◽  
Vol 288 (29) ◽  
pp. 20785-20796 ◽  
Author(s):  
Rebecca S. Cooper ◽  
Guillermo A. Altenberg
Keyword(s):  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Binding Domains ◽  
Partial Opening ◽  
Contact Models ◽  
Bacterial Lipid ◽  
Atp Binding Cassette

In ATP-binding cassette proteins, the two nucleotide-binding domains (NBDs) work as dimers to bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is controversial. It is still unresolved whether hydrolysis leads to dissociation of the ATP-induced dimers or partial opening of the dimers such that the NBDs remain in contact during the hydrolysis cycle. We studied the bacterial lipid flippase MsbA by luminescence resonance energy transfer (LRET). The LRET signal between optical probes reacted with single-cysteine mutants was employed to follow NBD association/dissociation in real time. The intermonomer distances calculated from LRET data indicate that the NBDs separate completely following ATP hydrolysis, even in the presence of mm MgATP, and that the dissociation occurs following each hydrolysis cycle. The results support association/dissociation, as opposed to constant contact models, for the mode of operation of ATP-binding cassette proteins.

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.

Nucleotide dependence of the dimerization of ATP binding cassette nucleotide binding domains

2016 ◽  
Vol 480 (2) ◽  
pp. 268-272 ◽  
Author(s):  
Gregory A. Fendley ◽  
Ina L. Urbatsch ◽  
Roger B. Sutton ◽  
Maria E. Zoghbi ◽  
Guillermo A. Altenberg
Keyword(s):  
Nucleotide Binding ◽  
Atp Binding ◽  
Binding Domains ◽  
Atp Binding Cassette

scholarly journals Simulation of the Coupling between Nucleotide Binding and Transmembrane Domains in the ATP Binding Cassette Transporter BtuCD

2007 ◽  
Vol 92 (8) ◽  
pp. 2727-2734 ◽  
Author(s):  
Jacob Sonne ◽  
Christian Kandt ◽  
Günther H. Peters ◽  
Flemming Y. Hansen ◽  
Morten Ø. Jensen ◽  
...  
Keyword(s):  
Nucleotide Binding ◽  
Transmembrane Domains ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

The Engine of ABC Proteins

Physiology ◽  
2003 ◽  
Vol 18 (5) ◽  
pp. 191-195 ◽  
Author(s):  
Guillermo A. Altenberg
Keyword(s):  
Molecular Mechanism ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Protein Families ◽  
Abc Proteins ◽  
Substrate Transport ◽  
Binding Domains ◽  
Atp Binding Cassette

Proteins that belong to the ATP-binding cassette superfamily span from bacteria to humans and comprise one of the largest protein families. These proteins are characterized by the presence of two nucleotide-binding domains, and recent studies suggest that association and dissociation of these domains is a common basic molecular mechanism of operation that couples ATP binding/hydrolysis to substrate transport across membranes.

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
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