Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis - PubMed (original) (raw)

. 1998 Mar 20;277(1):13-25.

doi: 10.1006/jmbi.1997.1589.

Affiliations

• PMID: 9514743
• DOI: 10.1006/jmbi.1997.1589

Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis

S Wolf et al. J Mol Biol. 1998.

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 arc 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.

Copyright 1998 Academic Press Limited.

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