5VKV
Solution NMR structure of the membrane electron transporter CcdA
Summary for 5VKV
| Entry DOI | 10.2210/pdb5vkv/pdb |
| NMR Information | BMRB: 30286 |
| Descriptor | Cytochrome c-type biogenesis protein CcdA (1 entity in total) |
| Functional Keywords | membrane transporter, oxidoreductase, dsbd |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| Total number of polymer chains | 1 |
| Total formula weight | 25292.14 |
| Authors | Zhou, Y.,Bushweller, J.H. (deposition date: 2017-04-24, release date: 2018-01-31, Last modification date: 2024-11-06) |
| Primary citation | Zhou, Y.,Bushweller, J.H. Solution structure and elevator mechanism of the membrane electron transporter CcdA. Nat. Struct. Mol. Biol., 25:163-169, 2018 Cited by PubMed Abstract: Membrane oxidoreductase CcdA plays a central role in supplying reducing equivalents from the bacterial cytoplasm to the envelope. It transports electrons across the membrane using a single pair of cysteines by a mechanism that has not yet been elucidated. Here we report an NMR structure of the Thermus thermophilus CcdA (TtCcdA) in an oxidized and outward-facing state. CcdA consists of two inverted structural repeats of three transmembrane helices (2 × 3-TM). We computationally modeled and experimentally validated an inward-facing state, which suggests that CcdA uses an elevator-type movement to shuttle the reactive cysteines across the membrane. CcdA belongs to the LysE superfamily, and thus its structure may be relevant to other LysE clan transporters. Structure comparisons of CcdA, semiSWEET, Pnu, and major facilitator superfamily (MFS) transporters provide insights into membrane transporter architecture and mechanism. PubMed: 29379172DOI: 10.1038/s41594-018-0022-z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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