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

Marcus J. Edwards, Nanakow A. 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

Research output: Contribution to journalArticlepeer-review

71 Scopus citations

Abstract

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
Number of pages5
JournalFEBS Letters
Volume588
Issue number10
DOIs
StatePublished - May 21 2014

Funding

DJR is a Royal Society Wolfson Foundation Merit Award holder. This research was supported by the Biotechnology and Biological Sciences Research Council ( BB/K00929X/1 and BB/H007288/1 ) and sponsored by the Subsurface Biogeochemical Research program (SBR)/Office of Biological and Environmental Research (BER) , U.S. Department of Energy (DOE) , and is a contribution of the Pacific Northwest National Laboratory (PNNL) Scientific Focus Area and the Mercury Scientific Focus Area at Oak Ridge National Laboratory (ORNL). The PNNL and ORNL are operated for the DOE by Battelle under contracts DE-AC05-76RLO1830 and DE-AC05-00OR22725

FundersFunder number
U.S. Department of Energy
Biological and Environmental Research
Oak Ridge National Laboratory
Pacific Northwest National Laboratory
Biotechnology and Biological Sciences Research CouncilBB/H007288/1, BB/K00929X/1

    Keywords

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

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