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Journal Article

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

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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: http://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]