Crystallization and preliminary X-ray crystallographic analysis of a putative agmatinase from Deinococcus radiodurans.
Agmatine, which results from the decarboxylation of arginine by arginine decarboxylase, is a metabolic intermediate in the biosynthesis of putresine and higher polyamines. The enzyme agmatinase catalyses the hydrolysis of agmatine to putresine and urea. Recent studies indicate that agmatinase plays important roles in mammals. Human mitochondrial agmatinase shows a considerable level of sequence similarity to bacterial agmatinases, including a putative agmatinase from Deinococcus radiodurans. The putative agmatinase from D. radiodurans has been overexpressed in Escherichia coli and crystallized at 297 K using polyethylene glycol 3000 as a precipitant. X-ray diffraction data were collected to 1.80 A from a crystal grown in the presence of Mn2+ and 1,6-hexanediamine. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2(1), with unit-cell parameters a = 81.77, b = 131.44, c = 168.85 A, alpha = beta = gamma = 90 degrees. A hexameric molecule is likely to be present in the asymmetric unit, giving a crystal volume per protein weight (VM) of 2.15 A3 Da(-1) and a solvent content of 41.8%.
Lee
Ji Ah
JA
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea.
Ahn
Hyung Jun
HJ
Ha
Jun Yong
JY
Shim
Sun Mi
SM
Kim
Kyoung Hoon
KH
Kim
Hye Kyung
HK
Suh
Se Won
SW
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D030562:Databases, Protein; D034301:Deinococcus / Q000201:enzymology*; D004926:Escherichia coli / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D014512:Ureohydrolases / Q000737:chemistry*
D011994:Recombinant Proteins; D014512:Ureohydrolases; C019625:agmatinase