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



ID: 318479.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Characterization of arc, a divergent member of the aaa atpase family from rhodococcus erythropolis
Authors:Wolf, S.; Nagy, I.; Lupas, A.; Pfeifer, G.; Cejka, Z.; Müller, S. A.; Engel, A.; Demot, R.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1998-03-20
Title of Journal:Journal of Molecular Biology
Volume:277
Issue / Number:1
Start Page:13
End Page:25
Audience:Not Specified
Abstract / Description:A gene encoding a AAA ATPase was discovered in the 5' region of the second operon of 20 S proteasome subunits in the nocardioform actinomycete Rhodococcus erythropolis NI86/21. The gene was cloned and expressed in Escherichia coli. The protein, ARC (AAA ATPase forming Ring-shaped Complexes), is a divergent member of the AAA family. The deduced product of the are gene is 591 residues long (66 kDa). The purified protein possesses a low, N-ethylmaleimide-sensitive ATPase activity and forms rings of six subunits, arranged symmetrically around a central opening or cavity. Two-dimensional crystals grown on lipid monolayers yielded images of the ATPase molecules in ''end-on'' orientation at 1.9 nm resolution. (C) 1998 Academic Press Limited. [References: 57]
Free Keywords:Aaa family; Clp; Hsp100; Atpase; Electron microscopy; Rhodococcus erythropolis.; Transmission electron-microscopy; Multiple alignment; Crystal-structure; Putative atpases; Inner membrane; 20s proteasome; Proteins; Complex; Yeast; Degradation.; Molecular biology & genetics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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