The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier
Open accessAbstract
Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open and matrix-open states. The structure of the cytoplasmic-open state is known, but it has proved difficult to understand the transport mechanism in the absence of a structure in the matrix-open state. Here, we describe the structure of the matrix-open state locked by bongkrekic acid bound in the ADP/ATP-binding site at the bottom of the central cavity. The cytoplasmic side of the carrier is closed by conserved hydrophobic residues, and a salt bridge network, braced by tyrosines. Glycine and small amino acid residues allow close-packing of helices on the matrix side. Uniquely, the carrier switches between states by rotation of its three domains about a fulcrum provided by the substrate-binding site. Because these features are highly conserved, this mechanism is likely to apply to the whole mitochondrial carrier family. VIDEO ABSTRACT.
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Metadata
- Authors
- Ruprecht, J. J., King, M. S., Zögg, T., Aleksandrova, A. A., Pardon, E., Crichton, P. G., Steyaert, J., & Kunji, E. R. S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2019-01
- Volume
- 176
- Issue
- 3
- Pages
- 435-447.e15
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2907890950
- Cited by
- 319
- References
- 51
- FWCI
- 11.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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