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6QYC

Crystal structure of MtrC from Shewanella baltica OS185

Summary for 6QYC
Entry DOI10.2210/pdb6qyc/pdb
DescriptorDecaheme c-type cytochrome, OmcA/MtrC family, HEME C, CALCIUM ION, ... (5 entities in total)
Functional Keywordscytochrome, membrane protein, greek key, multiheme, electron transport
Biological sourceShewanella baltica OS185
Total number of polymer chains3
Total formula weight211387.88
Authors
Clarke, T.A.,Edwards, M.J. (deposition date: 2019-03-08, release date: 2020-04-22, Last modification date: 2020-05-13)
Primary citationEdwards, 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: 32289252
DOI: 10.1016/j.cell.2020.03.032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.29 Å)
Structure validation

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