Expression, purification, crystallization and preliminary X-ray analysis of rat ecto-ADP-ribosyltransferase 2 (ART2.2).
ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety from NAD(+) onto proteins and other targets. These enzymes have been found in prokaryotes and in vertebrates; a eukaryotic enzyme structure is not yet known. The enzyme from Rattus norvegicus was expressed in the Escherichia coli periplasm at a level of about 0.2 mg per litre of culture, purified and crystallized. Native data sets were collected to 2.0 A resolution. A self-rotation function revealed a local twofold axis in crystal form A and a Patterson function showed a translational relationship in form B. Form C contains only one molecule in the asymmetric unit.
Mueller-Dieckmann
Christoph
C
Institut für Organische Chemie und Biochemie, Albertstrasse 21, Freiburg im Breisgau 79104, Germany.
Scheuermann
Till
T
Wursthorn
Karsten
K
Schröder
Jens
J
Haag
Friedrich
F
Schulz
Georg E
GE
Koch-Nolte
Friedrich
F
D036002:ADP Ribose Transferases / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D000945:Antigens, Differentiation, T-Lymphocyte; D002460:Cell Line; D006224:Cricetinae; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007313:Insecta; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D019897:Periplasm / Q000378:metabolism; D010957:Plasmids / Q000378:metabolism; D051381:Rats; D013696:Temperature; D013997:Time Factors
D000945:Antigens, Differentiation, T-Lymphocyte; D008562:Membrane Glycoproteins; D036002:ADP Ribose Transferases; C090163:Art2b protein, rat