4LM8
Crystal structure of the outer membrane decaheme cytochrome MtrC
Summary for 4LM8
Entry DOI | 10.2210/pdb4lm8/pdb |
Related | 3PMQ 3UCP 4LMH |
Descriptor | Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC, HEME C, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | greek key, c type cytochrome electron transport, outer membrane, electron transport |
Biological source | Shewanella oneidensis |
Total number of polymer chains | 1 |
Total formula weight | 81526.07 |
Authors | Clarke, T.A.,Edwards, M.J. (deposition date: 2013-07-10, release date: 2015-02-11, Last modification date: 2024-11-06) |
Primary citation | Edwards, M.J.,White, G.F.,Norman, M.,Tome-Fernandez, A.,Ainsworth, E.,Shi, L.,Fredrickson, J.K.,Zachara, J.M.,Butt, J.N.,Richardson, D.J.,Clarke, T.A. Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer. Sci Rep, 5:11677-11677, 2015 Cited by PubMed Abstract: Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism of electron exchange at the interface between cytochrome and acceptor is widely debated. The 1.8 Å x-ray crystal structure of the decaheme MtrC revealed a highly conserved CX8C disulfide that, when substituted for AX8A, severely compromised the ability of S. oneidensis to grow under aerobic conditions. Reductive cleavage of the disulfide in the presence of flavin mononucleotide (FMN) resulted in the reversible formation of a stable flavocytochrome. Similar results were also observed with other decaheme cytochromes, OmcA, MtrF and UndA. The data suggest that these decaheme cytochromes can transition between highly reactive flavocytochromes or less reactive cytochromes, and that this transition is controlled by a redox active disulfide that responds to the presence of oxygen. PubMed: 26126857DOI: 10.1038/srep11677 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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