Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism
| Autor: | Jochen Bürck, Anne S. Ulrich, Olga V. Nolandt, Siegmar Roth, Torsten H. Walther |
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| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Magnetic Resonance Spectroscopy Lipid Bilayers Molecular Sequence Data Biophysics Twin arginine translocation (Tat) Membrane protein Bacillus subtilis Biology Arginine Biochemistry Twin-arginine translocation pathway Escherichia coli Amino Acid Sequence Cloning Molecular Lipid bilayer TatCd Circular Dichroism Membrane Transport Proteins Cell Biology biology.organism_classification Circular dichroism (CD) Transmembrane protein Recombinant Proteins Membrane Membrane protein Thylakoid Oriented circular dichroism (OCD) |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788(10):2238-2244 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2009.07.003 |
| Popis: | The twin arginine translocation (Tat) system can transport fully folded proteins, including their cofactors, across bacterial and thylakoid membranes. The Tat system of Bacillus subtilis that serves to export the phosphodiesterase (PhoD) consists of only two membrane proteins, TatA(d) and TatC(d). The larger component TatC(d) has a molecular weight of 28 kDa and several membrane-spanning segments. This protein has been expressed in Escherichia coli and purified in sufficient amounts for structure analysis by circular dichroism (CD) and NMR spectroscopy. TatC(d) was reconstituted in detergent micelles and in lipid bilayers for CD analysis in solution and in macroscopically oriented samples, to examine the stability of the protein. Suitable protocols and model membrane systems have been established, by which TatC(d) maintains the level of helicity close to theoretically predicted, and its transmembrane alignment could been verified. |
| Databáze: | OpenAIRE |
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