2n4x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Transmembrane Electron Transporter CcdA== | |
| + | <StructureSection load='2n4x' size='340' side='right'caption='[[2n4x]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N4X FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n4x OCA], [https://pdbe.org/2n4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n4x RCSB], [https://www.ebi.ac.uk/pdbsum/2n4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n4x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O29205_ARCFU O29205_ARCFU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26389738</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2n4x" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chou | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Archaeoglobus fulgidus DSM 4304]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chou JJ]] | ||
| + | [[Category: Williamson JA]] | ||
Current revision
Structure of the Transmembrane Electron Transporter CcdA
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