English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structural features of archaebacterial and eukaryotic proteasomes

Koster, A. J., Walz, J., Lupas, A., & Baumeister, W. (1995). Structural features of archaebacterial and eukaryotic proteasomes. Molecular Biology Reports, 21(1), 11-20.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7369-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-736A-6
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Koster, A. J.1, Author              
Walz, J.1, Author              
Lupas, A.1, Author              
Baumeister, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              

Content

show
hide
Free keywords: Electron microscopy; Multicatalytic protease; Proteasome; Thermoplasma acidophilum.; Molecular-weight proteases; Rabbit reticulocyte lysate; Thermoplasma-acidophilum; Multicatalytic proteinase; Electron-microscopy; Prosome particle; Complex; Ubiquitin; Subunit; Purification.; Molecular biology & genetics.
 Abstract: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation. The molecule has a molecular mass of approximately 2000 kD and has a highly conserved structure in eukaryotes. The 26S proteasome is formed by a barrel-shaped 20S core complex and two polar 19S complexes. The 20S complex has C2 symmetry and is formed by four seven-membered rings of which the outer rings (alpha-type subunits) are rotated by 25.7 degrees relative to the inner rings while the inner rings (P-type subunits) are in register. From a comparison of the activity and regulation of the 26S and 20S particles it can be deduced that the 20S particle contains the protease activity while the 19S complex contains isopeptidase, ATPase and protein unfolding activities. In this article we describe the structures of various proteasome complexes as determined by electron microscopy and discuss structural implications of their subunit sequences. [References: 42]

Details

show
hide
Language(s):
 Dates: 1995
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 318612
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular Biology Reports
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 21 (1) Sequence Number: - Start / End Page: 11 - 20 Identifier: -