Ontology highlight
ABSTRACT:
SUBMITTER: Williamson JA
PROVIDER: S-EPMC7871232 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
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]