The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface
Journal Article
·
· FEBS Letters, 588(10):1886-1890
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 were arranged so the distance between heme-5 on adjacent OmcA monomers was less than 1 nm, 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 ~ 1 nm of mineral surface.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1136588
- Report Number(s):
- PNNL-SA-102427; KP1702030
- Journal Information:
- FEBS Letters, 588(10):1886-1890, Journal Name: FEBS Letters, 588(10):1886-1890
- Country of Publication:
- United States
- Language:
- English
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