Unknown

Dataset Information

0

Structure and multistate function of the transmembrane electron transporter CcdA.


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.

SUBMITTER: Williamson JA 

PROVIDER: S-EPMC7871232 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure and multistate function of the transmembrane electron transporter CcdA.

Williamson Jessica A JA   Cho Seung-Hyun SH   Ye Jiqing J   Collet Jean-Francois JF   Beckwith Jonathan R JR   Chou James J JJ  

Nature structural & molecular biology 20150921 10


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  ...[more]

Similar Datasets

| S-EPMC5805637 | biostudies-literature
| S-EPMC126151 | biostudies-literature
| S-EPMC7679968 | biostudies-literature
| S-EPMC7363144 | biostudies-literature
| S-EPMC3522279 | biostudies-literature
| S-EPMC8298354 | biostudies-literature
| S-EPMC6393857 | biostudies-literature
| S-EPMC6709370 | biostudies-literature
| S-EPMC94873 | biostudies-literature
| S-EPMC3061371 | biostudies-literature