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

Edwards, Marcus J, Baiden, Nanakow, Johs, Alexander, Tomanicek, Stephen J, Liang, Liyuan, Shi, Liang, Fredrickson, Jim K, Zachara, John M, Gates, Andrew J ORCID: https://orcid.org/0000-0002-4594-5038, Butt, Julea N ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A ORCID: https://orcid.org/0000-0002-6234-1914 (2014) The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface. FEBS Letters, 588 (10). pp. 1886-1890. ISSN 0014-5793

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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.

Item Type:	Article
Additional Information:	Copyright © 2014. Published by Elsevier B.V.
Uncontrolled Keywords:	multiheme cytochrome,mineral respiration,electron transfer,shewanella,c-type heme,outer membrane,metalloprotein
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science Faculty of Science > School of Chemistry Faculty of Science > School of Natural Sciences
Depositing User:	Pure Connector
Date Deposited:	12 May 2014 15:34
Last Modified:	23 Dec 2022 02:31
URI:	https://ueaeprints.uea.ac.uk/id/eprint/48431
DOI:	10.1016/j.febslet.2014.04.013

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