Structural basis of interprotein electron transfer in bacterial sulfite oxidation
| Autor: | Elise L Laming, G Patricia Casas Garcia, Aaron P. McGrath, Marc Kvansakul, Megan J. Maher, Benoit Calmes, Ulrike Kappler, Jill Trewhella, Graeme R. Hanson, J. Mitchell Guss, Paul V. Bernhardt |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Protein Conformation QH301-705.5 Science Crystallography X-Ray General Biochemistry Genetics and Molecular Biology Electron Transport chemistry.chemical_compound Electron transfer Protein structure molybdenum sulfite oxidase Sulfite Bacterial Proteins Oxidoreductase Sulfite oxidase sinorhizobium meliloti Sulfites structural biology Biology (General) chemistry.chemical_classification General Immunology and Microbiology Hydrogen bond General Neuroscience General Medicine Electron acceptor Biophysics and Structural Biology electron transfer Electron transport chain Crystallography Kinetics chemistry Biochemistry Thermodynamics Medicine Other Oxidoreductases Oxidation-Reduction Protein Binding Research Article |
| Zdroj: | eLife, Vol 4 (2015) eLife |
| Popis: | 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. DOI: http://dx.doi.org/10.7554/eLife.09066.001 eLife digest A key feature of many important chemical reactions in cells is the transfer of particles called electrons from one molecule to another. The sulfite oxidizing enzymes (or SOEs) are a group of enzymes that are found in many organisms. These enzymes convert sulfite, which is a very reactive compound that can damage cells, into another compound called sulfate. As part of this process the SOE transfers electrons from sulfite to other molecules, such as oxygen or a protein called cytochrome c. In the past, researchers have described the three-dimensional structure of three SOEs using a technique called X-ray crystallography. However, it has been difficult to study how SOEs pass electrons to other molecules because of the temporary nature of the interactions. McGrath et al. studied an SOE called SorT, which is found in bacteria. The SorT enzyme passes electrons from sulfite to another protein called SorU. McGrath used X-ray crystallography to determine the three-dimensional structures of versions of these proteins from a bacterium called Sinorhizobium meliloti. This included structures of the proteins on their own, and when they were bound to each other. These structures revealed that a subtle change in the shape of SorU occurs when the proteins interact, which enables an electron to be quickly transferred. McGrath et al. also found that the interface between the two proteins showed an unexpectedly high number of contact sites. These strengthen the interaction between the two proteins, which helps to make electron transfer more efficient. However, these contact sites do not prevent the two proteins from quickly moving apart after the electrons have been transferred. The next challenge is to find out whether these observations are common to SOEs from other forms of life. DOI: http://dx.doi.org/10.7554/eLife.09066.002 |
| Databáze: | OpenAIRE |
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