6GCI
Structure of the bongkrekic acid-inhibited mitochondrial ADP/ATP carrier
Summary for 6GCI
| Entry DOI | 10.2210/pdb6gci/pdb |
| Descriptor | mitochondrial ADP/ATP carrier, Nanobody, Bongkrekic acid, ... (5 entities in total) |
| Functional Keywords | transporter, inhibitor, mitochondrial, carrier, membrane protein |
| Biological source | Thermothelomyces thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) More |
| Total number of polymer chains | 2 |
| Total formula weight | 56653.63 |
| Authors | Ruprecht, J.J.,King, M.S.,Pardon, E.,Aleksandrova, A.A.,Zogg, T.,Crichton, P.G.,Steyaert, J.,Kunji, E.R.S. (deposition date: 2018-04-17, release date: 2019-01-09, Last modification date: 2024-11-13) |
| Primary citation | Ruprecht, J.J.,King, M.S.,Zogg, T.,Aleksandrova, A.A.,Pardon, E.,Crichton, P.G.,Steyaert, J.,Kunji, E.R.S. The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier. Cell, 176:435-447.e15, 2019 Cited by PubMed Abstract: 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. PubMed: 30611538DOI: 10.1016/j.cell.2018.11.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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