Functional asymmetry of the two nucleotide binding domains in the ABC transporter Ste6

2001 ◽  
Vol 264 (6) ◽  
pp. 883-893 ◽  
Author(s):  
C. Proff ◽  
R. Kölling
Keyword(s):  
Abc Transporter ◽  
Nucleotide Binding ◽  
Functional Asymmetry ◽  
Binding Domains

ATP-Induced Conformational Changes of Nucleotide-Binding Domains in an ABC Transporter. Importance of the Water-Mediated Entropic Force

2014 ◽  
Vol 118 (44) ◽  
pp. 12612-12620 ◽  
Author(s):  
Tomohiko Hayashi ◽  
Shuntaro Chiba ◽  
Yusuke Kaneta ◽  
Tadaomi Furuta ◽  
Minoru Sakurai
Keyword(s):  
Abc Transporter ◽  
Conformational Changes ◽  
Nucleotide Binding ◽  
Entropic Force ◽  
Binding Domains

scholarly journals Movement of the Nucleotide Binding Domains in the ABC Transporter MsbA Reconstituted in Nanodiscs

2015 ◽  
Vol 108 (2) ◽  
pp. 145a
Author(s):  
Maria E. Zoghbi ◽  
Guillermo A. Altenberg
Keyword(s):  
Abc Transporter ◽  
Nucleotide Binding ◽  
Binding Domains

scholarly journals Domain Interactions in the Yeast ATP Binding Cassette Transporter Ycf1p: Intragenic Suppressor Analysis of Mutations in the Nucleotide Binding Domains

2001 ◽  
Vol 183 (16) ◽  
pp. 4761-4770 ◽  
Author(s):  
Juan M. Falcón-Pérez ◽  
Mónica Martı́nez-Burgos ◽  
Jesús Molano ◽  
Marı́a J. Mazón ◽  
Pilar Eraso
Keyword(s):  
Atpase Activity ◽  
Abc Transporter ◽  
Transmembrane Domain ◽  
Substrate Binding ◽  
Nucleotide Binding ◽  
Intramolecular Interactions ◽  
Phenotypic Characterization ◽  
Atp Binding ◽  
Binding Domains ◽  
Atp Binding Cassette

ABSTRACT The yeast cadmium factor (Ycf1p) is a vacuolar ATP binding cassette (ABC) transporter required for heavy metal and drug detoxification. Cluster analysis shows that Ycf1p is strongly related to the human multidrug-associated protein (MRP1) and cystic fibrosis transmembrane conductance regulator and therefore may serve as an excellent model for the study of eukaryotic ABC transporter structure and function. Identifying intramolecular interactions in these transporters may help to elucidate energy transfer mechanisms during transport. To identify regions in Ycf1p that may interact to couple ATPase activity to substrate binding and/or movement across the membrane, we sought intragenic suppressors of ycf1 mutations that affect highly conserved residues presumably involved in ATP binding and/or hydrolysis. Thirteen intragenic second-site suppressors were identified for the D777N mutation which affects the invariant Asp residue in the Walker B motif of the first nucleotide binding domain (NBD1). Two of the suppressor mutations (V543I and F565L) are located in the first transmembrane domain (TMD1), nine (A1003V, A1021T, A1021V, N1027D, Q1107R, G1207D, G1207S, S1212L, and W1225C) are found within TMD2, one (S674L) is in NBD1, and another one (R1415G) is in NBD2, indicating either physical proximity or functional interactions between NBD1 and the other three domains. The original D777N mutant protein exhibits a strong defect in the apparent affinity for ATP and V max of transport. The phenotypic characterization of the suppressor mutants shows that suppression does not result from restoring these alterations but rather from a change in substrate specificity. We discuss the possible involvement of Asp777 in coupling ATPase activity to substrate binding and/or transport across the membrane.

scholarly journals Exploring conformational equilibria of a heterodimeric ABC transporter

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
M Hadi Timachi ◽  
Cedric AJ Hutter ◽  
Michael Hohl ◽  
Tufa Assafa ◽  
Simon Böhm ◽  
...  
Keyword(s):  
Binding Site ◽  
High Temperatures ◽  
Abc Transporter ◽  
Thermotoga Maritima ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Molecular Feature ◽  
Atp Binding Site ◽  
Binding Domains ◽  
Conformational Equilibria

ABC exporters pump substrates across the membrane by coupling ATP-driven movements of nucleotide binding domains (NBDs) to the transmembrane domains (TMDs), which switch between inward- and outward-facing (IF, OF) orientations. DEER measurements on the heterodimeric ABC exporter TM287/288 from Thermotoga maritima, which contains a non-canonical ATP binding site, revealed that in the presence of nucleotides the transporter exists in an IF/OF equilibrium. While ATP binding was sufficient to partially populate the OF state, nucleotide trapping in the pre- or post-hydrolytic state was required for a pronounced conformational shift. At physiologically high temperatures and in the absence of nucleotides, the NBDs disengage asymmetrically while the conformation of the TMDs remains unchanged. Nucleotide binding at the degenerate ATP site prevents complete NBD separation, a molecular feature differentiating heterodimeric from homodimeric ABC exporters. Our data suggest hydrolysis-independent closure of the NBD dimer, which is further stabilized as the consensus site nucleotide is committed to hydrolysis.

Water-mediated forces between the nucleotide binding domains generate the power stroke in an ABC transporter

2014 ◽  
Vol 616-617 ◽  
pp. 165-170 ◽  
Author(s):  
Tomoka Furukawa-Hagiya ◽  
Norio Yoshida ◽  
Shuntaro Chiba ◽  
Tomohiko Hayashi ◽  
Tadaomi Furuta ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Nucleotide Binding ◽  
Power Stroke ◽  
Binding Domains
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