2N4X
Structure of the Transmembrane Electron Transporter CcdA
Summary for 2N4X
| Entry DOI | 10.2210/pdb2n4x/pdb |
| NMR Information | BMRB: 25685 |
| Descriptor | Cytochrome C-type biogenesis protein (CcdA) (1 entity in total) |
| Functional Keywords | transmembrane electron transporter, transmembrane reductase, ccda, dsbd homolog, membrane protein |
| Biological source | Archaeoglobus fulgidus DSM 4304 |
| Total number of polymer chains | 1 |
| Total formula weight | 22771.21 |
| Authors | Chou, J.J.,Williamson, J.A. (deposition date: 2015-07-01, release date: 2016-05-18, Last modification date: 2024-05-15) |
| Primary citation | Williamson, J.A.,Cho, S.H.,Ye, J.,Collet, J.F.,Beckwith, J.R.,Chou, J.J. Structure and multistate function of the transmembrane electron transporter CcdA. Nat.Struct.Mol.Biol., 22:809-814, 2015 Cited by PubMed Abstract: The mechanism by which transmembrane reductases use a single pair of cysteine residues to relay electrons between protein substrates across biological membranes is a long-standing mystery in thiol-redox biochemistry. Here we show the NMR structure of a reduced-state mimic of archaeal CcdA, a protein that transfers electrons across the inner membrane, by using a redox-active NMR sample. The two cysteine positions in CcdA are separated by 20 Å. Whereas one is accessible to the cytoplasm, the other resides in the protein core, thus implying that conformational exchange is required for periplasmic accessibility. In vivo mixed disulfide-trapping experiments validated the functional positioning of the cysteines, and in vitro accessibility results confirmed conformational exchange. Our NMR and functional data together show the existence of multiple conformational states and suggest a four-state model for relaying electrons from cytosolic to periplasmic redox substrates. PubMed: 26389738DOI: 10.1038/nsmb.3099 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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