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| Subject Categories: Structural Biology | Membranes & Transport |
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| The EMBO Journal
(2005) 24, 875–884, doi:10.1038/sj.emboj.7600565 Published online 3 February 2005 |
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| Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization |
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| Andrew P Turnbull1, 2, Daniel Kümmel1, Bianka Prinz3, 4, Caterina Holz3, 4, Jeffrey Schultchen3, 4, Christine Lang3, 4, Frank H Niesen4, 5, Klaus-Peter Hofmann5, Heinrich Delbrück4, 6, Joachim Behlke1, Eva-Christina Müller1, Ernst Jarosch1, Thomas Sommer1 and Udo Heinemann1, 6 |
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1 Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany 2 Protein Structure Factory, c/o BESSY GmbH, Berlin, Germany 3 Institut für Biotechnologie, FG Mikrobiologie und Genetik, Technische Universität Berlin, Berlin, Germany 4 Protein Structure Factory, Heubnerweg, Berlin, Germany 5 Institut für Medizinische Physik und Biophysik, Charité Universitätsmedizin Berlin, Berlin, Germany 6 Institut für Chemie/Kristallographie, Freie Universität Berlin, Berlin, Germany To whom correspondence should be addressed Udo Heinemann, Max-Delbrück-Centrum für Molekulare Medizin, Forschungsgruppe Kristallographie, Robert-Rössle-Stra  e 10, 13092 Berlin, Germany. Tel.: +49 30 9406 3420; Fax: +49 30 9406 2548; E-mail: heinemann@mdc-berlin.de
Received 24 August 2004; Accepted 4 January 2005; Published online 3 February 2005. |
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| Abstract |
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BET3 is a component of TRAPP, a complex involved in the tethering of transport vesicles to the cis-Golgi membrane. The crystal structure of human BET3 has been determined to 1.55-Å resolution. BET3 adopts an  / -plait fold and forms dimers in the crystal and in solution, which predetermines the architecture of TRAPP where subunits are present in equimolar stoichiometry. A hydrophobic pocket within BET3 buries a palmitate bound through a thioester linkage to cysteine 68. BET3 and yeast Bet3p are palmitoylated in recombinant yeast cells, the mutant proteins BET3 C68S and Bet3p C80S remain unmodified. Both BET3 and BET3 C68S are found in membrane and cytosolic fractions of these cells; in membrane extractions, they behave like tightly membrane-associated proteins. In a deletion strain, both Bet3p and Bet3p C80S rescue cell viability. Thus, palmitoylation is neither required for viability nor sufficient for membrane association of BET3, which may depend on protein–protein contacts within TRAPP or additional, yet unidentified modifications of BET3. A conformational change may facilitate palmitoyl extrusion from BET3 and allow the fatty acid chain to engage in intermolecular hydrophobic interactions. |
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| Keywords: /-plait, BET3 protein, protein palmitoylation, TRAPP complex, vesicle tethering |
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