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A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77721

Baumeister,  W.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Rockel, B., Peters, J., Kühlmorgen, B., Glaeser, R. M., & Baumeister, W. (2002). A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy. EMBO Journal, 21(22), 5979-5984.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6DDE-6
Zusammenfassung
Tripeptidyl peptidase II (TPP II) is an exopeptidase of the subtilisin type of serine proteases that is thought to act downstream of the proteasome in the ubiquitin-proteasome pathway. Recently, a key role in a pathway parallel to the ubiquitin-proteasome pathway has been ascribed to TPP 11, which forms a giant protease complex in mammalian cells. Here, we report the 900-fold purification of TPP II from Drosophila eggs and demonstrate via cryo-electron microscopy that TPP II from Drosophila melanogaster also forms a giant protease complex. The presented three-dimensional reconstruction of the 57 X 27 nm TPP II complex at 3.3 nm resolution reveals that the 150 kDa subunits form a superstructure composed of two segmented and twisted strands. Each strand is 12.5 nm in width and composed of 11 segments that enclose a central channel.