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

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.

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Genre: Zeitschriftenartikel
Alternativer Titel : Embo J.

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 Urheber:
Rockel, B.1, Autor           
Peters, J.1, Autor           
Kühlmorgen, B., Autor
Glaeser, R. M., Autor
Baumeister, W.2, Autor           
Affiliations:
1External Organizations, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Schlagwörter: cryo-electron microscopy; three-dimensional reconstruction; tripeptidyl peptidase II
 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.

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Sprache(n): eng - English
 Datum: 2002-11-15
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 41668
ISI: 000179446900004
 Art des Abschluß: -

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Titel: EMBO Journal
  Alternativer Titel : Embo J.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 21 (22) Artikelnummer: - Start- / Endseite: 5979 - 5984 Identifikator: ISSN: 0261-4189