Structure and function of the C-terminal domain of MrpA in theBacillus subtilisMrp-antiporter complex - The evolutionary progenitor of the long horizontal helix in complex I
| Autor: | Kamil Górecki, Yusra Al-Eryani, Vamsi K. Moparthi, Egle Virzintiene, Leonard T. Shumbe, Cecilia Hägerhäll |
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| Rok vydání: | 2013 |
| Předmět: |
Antiporter
Protein subunit Cytochrome c Biophysics Bacillus subtilis Biochemistry Bacterial Proteins Structural Biology Complex I Genetics NuoL NuoJ Molecular Biology biology C-terminus MrpA Cell Biology Hydrogen-Ion Concentration biology.organism_classification Transmembrane protein Protein Structure Tertiary Transmembrane domain Mrp-antiporter complex Helix Function (biology) |
| Zdroj: | FEBS Letters. 587:3341-3347 |
| ISSN: | 0014-5793 |
| Popis: | MrpA and MrpD are homologous to NuoL, NuoM and NuoN in complex I over the first 14 transmembrane helices. In this work, the C-terminal domain of MrpA, outside this conserved area, was investigated. The transmembrane orientation was found to correspond to that of NuoJ in complex I. We have previously demonstrated that the subunit NuoK is homologous to MrpC. The function of the MrpA C-terminus was tested by expression in a previously used Bacillus subtilis model system. At neutral pH, the truncated MrpA still worked, but at pH 8.4, where Mrp-complex formation is needed for function, the C-terminal domain of MrpA was absolutely required. |
| Databáze: | OpenAIRE |
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