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Investigations on the maturation and regulation of archaebacterial proteasomes

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78033

Groll,  M.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77801

Brandstetter,  H.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77711

Bartunik,  H.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Groll, M., Brandstetter, H., Bartunik, H., Bourenkow, G., & Huber, R. (2003). Investigations on the maturation and regulation of archaebacterial proteasomes. Journal of Molecular Biology, 327(1), 75-83.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6C69-5
Zusammenfassung
The 20 S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25 Angstrom resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20 S proteasomes. While eukaryotic CPs are auto-inhibited by the N- terminal tails of the outer a-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A. fulgidus leaving a pore leading into the particle with a diameter of 13 Angstrom. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20 S proteasome. (C) 2003 Elsevier Science Ltd. All rights reserved.