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EMBO reports 6, 8, 787–793 (2005)
doi:10.1038/sj.embor.7400463
Published online: 15 July 2005
The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex
Daniel Kümmel1, 2, Jürgen J Müller1, Yvette Roske1, 3, Rolf Misselwitz1, Konrad Büssow3, 4 & Udo Heinemann1, 2
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1 Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13092 Berlin, Germany
2 Chemistry Institute, Free University, Takustrasse 6, 14195 Berlin, Germany
3 Protein Structure Factory, Heubnerweg 6, 14059 Berlin, Germany
4 Max Planck Institute for Molecular Genetics, Ihnestrasse 73, 14195 Berlin, Germany
To whom correspondence should be addressed
Udo Heinemann Tel: +49 30 9406 3420; Fax: +49 30 9406 2548; E-mail: heinemann@mdc-berlin.de
Received 21 February 2005; Accepted 25 May 2005; Published online 15 July 2005.
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Abstract
The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Å crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an  / -plait topology and forms a dimer. In spite of low sequence similarity, the structure of TPC6 strikingly resembles that of BET3. The similarity is especially prominent at the dimerization interfaces of the proteins. This suggests heterodimerization of TPC6 and BET3, which is shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family of paralogous proteins with closely similar three-dimensional structures but little sequence similarity among its members.
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