The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface

Marcus J Edwards, Nanakow Baiden, Alexander Johs, Stephen J Tomanicek, Liyuan Liang, Liang Shi, Jim K Fredrickson, John M Zachara, Andrew J Gates, Julea N Butt, David J Richardson, Thomas A Clarke

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The X-ray crystal structure of Shewanella oneidensis OmcA, an extracellular decaheme cytochrome involved in mineral reduction, was solved to a resolution of 2.7 Å. The four OmcA molecules in the asymmetric unit are arranged so the minimum distance between heme 5 on adjacent OmcA monomers is 9 Å, indicative of a transient OmcA dimer capable of intermolecular electron transfer. A previously identified hematite binding motif was identified near heme 10, forming a hydroxylated surface that would bring a heme 10 electron egress site to ∼ 10 Å of a mineral surface.
Original languageEnglish
Pages (from-to)1886-1890
JournalFEBS Letters
Issue number10
Publication statusPublished - 21 May 2014


  • Multiheme cytochrome
  • Mineral respiration
  • Electron transfer
  • Shewanella
  • c-Type heme
  • Outer membrane
  • Metalloprotein

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