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.; Engel, A.; Demot, R.; Baumeister, W.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7220-3

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]