Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe-Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed example of an Fe-Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 A and have the symmetry of space group P6(5)22, with one dimer per asymmetric unit. Diffraction data collected using a conventional X--ray source from a cryocooled crystal extend to 2.90 A resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.
Schenk
G
G
Department of Biochemistry, The University of Queensland, Brisbane, QLD 4072, Australia.
Carrington
L E
LE
Hamilton
S E
SE
de Jersey
J
J
Guddat
L W
LW
D000135:Acid Phosphatase / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification*; D007501:Iron / Q000737:chemistry; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification*; D008345:Manganese / Q000737:chemistry; D019657:Solanaceae / Q000201:enzymology*
D006023:Glycoproteins; D007527:Isoenzymes; D008345:Manganese; D007501:Iron; C091137:purple acid phosphatase; D000135:Acid Phosphatase