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  Characterization of arc, a divergent member of the aaa atpase family from rhodococcus erythropolis

Wolf, S., Nagy, I., Lupas, A., Pfeifer, G., Cejka, Z., Müller, S. A., et al. (1998). Characterization of arc, a divergent member of the aaa atpase family from rhodococcus erythropolis. Journal of Molecular Biology, 277(1), 13-25.

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 Creators:
Wolf, S.1, Author              
Nagy, I.1, Author              
Lupas, A.1, Author              
Pfeifer, G.1, Author              
Cejka, Z., Author
Müller, S. A., Author
Engel, A., Author
Demot, R., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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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.
 Abstract: 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]

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 Dates: 1998-03-20
 Publication Status: Published in print
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 Identifiers: eDoc: 318479
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 277 (1) Sequence Number: - Start / End Page: 13 - 25 Identifier: -