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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents

ID: 41668.0, MPI für Biochemie / Structural Biology (W. Baumeister)
A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy
Authors:Rockel, B.; Peters, J.; Kühlmorgen, B.; Glaeser, R. M.; Baumeister, W.
Date of Publication (YYYY-MM-DD):2002-11-15
Title of Journal:EMBO Journal
Journal Abbrev.:Embo J.
Issue / Number:22
Start Page:5979
End Page:5984
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Free Keywords:cryo-electron microscopy; three-dimensional reconstruction; tripeptidyl peptidase II
Comment of the Author/Creator:Date: 2002, NOV 15
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Molecular Structural Biology (W. Baumeister)
External Affiliations:Univ Calif Berkeley, Lawrence Berkeley Lab, Div Life Sci, Berkeley, CA 94720 USA
Identifiers:ISI:000179446900004 [ID No:1]
ISSN:0261-4189 [ID No:2]
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