6R2Q
Structure of the Mtr complex
Summary for 6R2Q
| Entry DOI | 10.2210/pdb6r2q/pdb |
| Related | 6QYC |
| Descriptor | Cystathionine beta-synthase, Uncharacterized protein, Decaheme c-type cytochrome, OmcA/MtrC family, ... (6 entities in total) |
| Functional Keywords | cytochrome, membrane protein, greek key, multiheme, electron transport |
| Biological source | Shewanella baltica More |
| Total number of polymer chains | 3 |
| Total formula weight | 194121.75 |
| Authors | Clarke, T.A.,Edwards, M.J. (deposition date: 2019-03-18, release date: 2020-04-22, Last modification date: 2020-05-13) |
| Primary citation | Edwards, M.J.,White, G.F.,Butt, J.N.,Richardson, D.J.,Clarke, T.A. The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire. Cell, 181:665-673.e10, 2020 Cited by PubMed Abstract: A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand β-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes. PubMed: 32289252DOI: 10.1016/j.cell.2020.03.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.697 Å) |
Structure validation
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