Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis.
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.
Wolf
S
S
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried, D-82152, Germany.
Nagy
I
I
Lupas
A
A
Pfeifer
G
G
Cejka
Z
Z
Müller
S A
SA
Engel
A
A
De Mot
R
R
Baumeister
W
W
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D008854:Microscopy, Electron / Q000379:methods; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012097:Repressor Proteins; D012240:Rhodococcus / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D009711:Nucleotides; D011994:Recombinant Proteins; D012097:Repressor Proteins; C041610:arcA protein, E coli