Wolf S, Nagy I, Lupas A, Pfeifer G, Cejka Z, Müller S A, Engel A, De Mot R, Baumeister W
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried, D-82152, Germany.
J Mol Biol. 1998 Mar 20;277(1):13-25. doi: 10.1006/jmbi.1997.1589.
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.
在诺卡氏放线菌红平红球菌NI86/21的20S蛋白酶体亚基第二个操纵子的5'区域发现了一个编码AAA型ATP酶的基因。该基因被克隆并在大肠杆菌中表达。ARC蛋白（形成环形复合物的AAA型ATP酶）是AAA家族的一个不同成员。arc基因推导的产物长591个氨基酸残基（66 kDa）。纯化后的蛋白具有低水平的、对N-乙基马来酰亚胺敏感的ATP酶活性，并形成由六个亚基组成的环，围绕着一个中央开口或腔对称排列。在脂质单层上生长的二维晶体以1.9 nm的分辨率产生了ATP酶分子“端对端”取向的图像。
