Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum.
DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase derived from Corynebacterium glutamicum, was crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant. The crystal belongs to the trigonal system with space group R32 and contains three subunits in the asymmetric unit. A molecular-replacement solution was found using the structure of transcarboxylase 12S from Propionibacterium shermanii as a search model.
Yamada
Minoru
M
Materials Science and Engineering, Graduate School of Engineering, Tokyo Denki University, 2-2 Nishiki-cho, Kanda, Chiyoda-ku, Tokyo 101-8457, Japan.
Natsume
Ryo
R
Nakamatsu
Tsuyoshi
T
Horinouchi
Sueharu
S
Kawasaki
Hisashi
H
Senda
Toshiya
T
D000103:Acetyl-CoA Carboxylase / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D048230:Corynebacterium glutamicum / Q000201:enzymology* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D021122:Protein Subunits
D001426:Bacterial Proteins; D021122:Protein Subunits; D000103:Acetyl-CoA Carboxylase