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Elife. 2015 Dec 19;4:e09066. doi: 10.7554/eLife.09066.

Structural basis of interprotein electron transfer in bacterial sulfite oxidation.

Author information

1
Structural Biology Program, Centenary Institute, Sydney, Australia.
2
School of Molecular Bioscience, University of Sydney, Sydney, Australia.
3
Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Australia.
4
Centre for Metals in Biology, The University of Queensland, Brisbane, Australia.
5
School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia.
6
Centre for Advanced Imaging, University of Queensland, Brisbane, Australia.

Abstract

Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 ± 0.8 μM. The crystal structures of the oxidized SorT and SorU, both in isolation and in complex, reveal the interface to be remarkably electrostatic, with an unusually large number of direct hydrogen bonding interactions. The assembly of the complex is accompanied by an adjustment in the structure of SorU, and conformational sampling provides a mechanism for dissociation of the SorT/SorU assembly.

KEYWORDS:

Sinorhizobium meliloti; biophysics; electron transfer; molybdenum; structural biology; sulfite oxidase

PMID:
26687009
PMCID:
PMC4760952
DOI:
10.7554/eLife.09066
[Indexed for MEDLINE]
Free PMC Article

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