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



ID: 318521.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from the archaeon thermoplasma acidophilum
Authors:Pamnani, V.; Tamura, T.; Lupas, A.; Peters, J.; Cejka, Z.; Ashraf, W.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1997-03-10
Title of Journal:FEBS Letters
Volume:404
Issue / Number:2-3
Start Page:263
End Page:268
Audience:Not Specified
Abstract / Description:A member of the AAA family of Mg2+-ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (M(r) 83 000), which has an optimal Mg2+-ATPase activity at 70 degrees C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings, Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL. (C) 1997 Federation of European Biochemical Societies. [References: 42]
Free Keywords:Aaa family; Atpase; Cdc48; p97; Archaea; Thermoplasma acidophilum.; Protein secondary structure; Putative atpases; Cell-cycle; Escherichia-coli; Gene-expression; Family; Yeast; Prediction; Complex; Member.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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