S3.8 Effects of inhibitors on the unfolding of the mitochondrial ADP/ATP carrier by single-molecule force spectroscopy

Hellawell, Alex M.; Kedrov, Alexej; Kłosin, Adam; Broadhurst, R. William; Kunji, Edmund R.S.; Müller, Daniel J.

doi:10.1016/j.bbabio.2008.05.107

Cited by 1 publication

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“…A β--D--glucoside ring is consistent with the crystal structure of ATR [80] and NMR studies of CATR and ATR [81]. CATR differs from ATR by one carboxylate group that gives extra resistance to unfolding of yeast Aac3p by single--molecule force spectroscopy, which was located to transmembrane H2, again consistent with a β--D--glucoside ring [80,81]. It was noted first in the bovine structure that the odd--numbered α--helices have a pronounced L--shape [68].…”

Section: The Atomic Structures Of the Bovine And Yeast Adp/atp Carriersupporting

confidence: 77%

“…In the yeast structures CATR was modelled with a β--D--glucoside ring [67] (Figure 5), rather than the α--D--glucoside in the bovine structure [68,69]. A β--D--glucoside ring is consistent with the crystal structure of ATR [80] and NMR studies of CATR and ATR [81]. CATR differs from ATR by one carboxylate group that gives extra resistance to unfolding of yeast Aac3p by single--molecule force spectroscopy, which was located to transmembrane H2, again consistent with a β--D--glucoside ring [80,81].…”

Section: The Atomic Structures Of the Bovine And Yeast Adp/atp Carriersupporting

confidence: 57%

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The transport mechanism of the mitochondrial ADP/ATP carrier

Kunji

Aleksandrova

King

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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124

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The mitochondrial ADP/ATP carrier imports ADP from the cytosol and exports ATP from the mitochondrial matrix, providing key steps in oxidative phosphorylation in eukaryotic organisms. The transport protein belongs to the mitochondrial carrier family, a large transporter family in the inner membrane of mitochondria. It is one of the best studied members of the family and serves as a paradigm for the molecular mechanism of mitochondrial carriers. Structurally, the carrier consists of three homologous domains, each composed of two transmembrane α--helices linked with a loop and short α--helix on the matrix side. The transporter cycles between a cytoplasmic and matrix conformation in which a central substrate binding site is alternately accessible to these compartments for binding of ADP or ATP. On both the cytoplasmic and matrix side of the carrier are networks consisting of three salt bridges each. In the cytoplasmic conformation, the matrix salt bridge network is formed and the cytoplasmic network is disrupted, opening the central substrate binding site to the intermembrane space and cytosol, whereas the converse occurs in the matrix conformation. In the transport cycle, tighter substrate binding in the intermediate states allows the interconversion of conformations by lowering the energy barrier for disruption and formation of these networks, opening and closing the carrier to either side of the membrane in an alternating way. The simultaneous 2 rotation of three domains around a central translocation pathway constitutes a unique mechanism among transport proteins.

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