2n4x | pdb_00002n4x

Structure of the Transmembrane Electron Transporter CcdA

spinqualitylabelsall models 2n4x Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n4x is a 1 chain structure with sequence from Archaeoglobus fulgidus DSM 4304. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O29205_ARCFU Publication Abstract from PubMed 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 A. 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. Structure and multistate function of the transmembrane electron transporter CcdA.,Williamson JA, Cho SH, Ye J, Collet JF, Beckwith JR, Chou JJ Nat Struct Mol Biol. 2015 Oct;22(10):809-14. doi: 10.1038/nsmb.3099. Epub 2015, Sep 21. PMID:26389738 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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