%0 Journal Article %1 muller_structural_2007 %A Müller, Sonja D %A De Angelis, Anna A %A Walther, Torsten H %A Grage, Stephan L %A Lange, Christian %A Opella, Stanley J %A Ulrich, Anne S %D 2007 %J Biochim. Biophys. Acta %K Acid Amino Data Proteins,Computer Proteins,Molecular Resonance Sequence Sequence,Bacillus Simulation,Magnetic Spectroscopy,Membrane Transport subtilis,Bacterial %N 12 %P 3071--3079 %R 10.1016/j.bbamem.2007.09.008 %T Structural characterization of the pore forming protein \TatAd\ of the twin-arginine translocase in membranes by solid-state 15N-\NMR\ %V 1768 %X The transmembrane protein TatA is the pore forming unit of the twin-arginine translocase (Tat), which has the unique ability of transporting folded proteins across the cell membrane. This ATP-independent protein export pathway is a recently discovered alternative to the general secretory (Sec) system of bacteria. To obtain insight in the translocation mechanism, the structure and alignment in the membrane of the well-folded segments 2-45 of TatAd from Bacillus subtilis was studied here. Using solid-state NMR in bicelles containing anionic lipids, the topology and orientation of TatAd was determined in an environment mimicking the bacterial membrane. A wheel-like pattern, characteristic for a tilted transmembrane helix, was observed in 15N chemical shift /15N-1H dipolar coupling correlation NMR spectra. Analysis of this PISA wheel revealed a 14-16 residue long N-terminal membrane-spanning helix which is tilted by 17 degrees with respect to the membrane normal. In addition, comparison of uniformly and selectively 15N-labeled TatA2-45 samples allowed determination of the helix polarity angle.

@article{muller_structural_2007, abstract = {The transmembrane protein TatA is the pore forming unit of the twin-arginine translocase (Tat), which has the unique ability of transporting folded proteins across the cell membrane. This ATP-independent protein export pathway is a recently discovered alternative to the general secretory (Sec) system of bacteria. To obtain insight in the translocation mechanism, the structure and alignment in the membrane of the well-folded segments 2-45 of TatAd from Bacillus subtilis was studied here. Using solid-state NMR in bicelles containing anionic lipids, the topology and orientation of TatAd was determined in an environment mimicking the bacterial membrane. A wheel-like pattern, characteristic for a tilted transmembrane helix, was observed in 15N chemical shift /15N-1H dipolar coupling correlation NMR spectra. Analysis of this PISA wheel revealed a 14-16 residue long N-terminal membrane-spanning helix which is tilted by 17 degrees with respect to the membrane normal. In addition, comparison of uniformly and selectively 15N-labeled TatA2-45 samples allowed determination of the helix polarity angle.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {M{\"{u}}ller, Sonja D and {De Angelis}, Anna A and Walther, Torsten H and Grage, Stephan L and Lange, Christian and Opella, Stanley J and Ulrich, Anne S}, biburl = {https://www.bibsonomy.org/bibtex/2bd20731f00c799cc21bfd6bf1ba5123c/nmrresource}, doi = {10.1016/j.bbamem.2007.09.008}, interhash = {9c0cfb6ed84147c827d631396990c92c}, intrahash = {bd20731f00c799cc21bfd6bf1ba5123c}, issn = {0006-3002}, journal = {Biochim. Biophys. Acta}, keywords = {Acid Amino Data Proteins,Computer Proteins,Molecular Resonance Sequence Sequence,Bacillus Simulation,Magnetic Spectroscopy,Membrane Transport subtilis,Bacterial}, month = dec, number = 12, pages = {3071--3079}, pmid = {17980349}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Structural characterization of the pore forming protein {\{}TatAd{\}} of the twin-arginine translocase in membranes by solid-state 15N-{\{}NMR{\}}}}, volume = 1768, year = 2007 }