Crystallization and preliminary crystallographic studies of the precursor and mature forms of a neutral lipase from the fungus Rhizopus delemar.
A neutral lipase from the filamentous fungus Rhizopus delemar has been crystallized in both its proenzyme and mature forms. Although the latter crystallizes readily and produces a variety of crystal forms, only one was found to be suitable for X-ray studies. It is monoclinic (C2, a = 92.8 A, b = 128.9 A, c = 78.3 A, beta = 135.8) with two molecules in the asymmetric unit related by a noncrystallographic diad. The prolipase crystals are orthorhombic (P2(1)2(1)2(1), with a = 79.8 A, b = 115.2 A, c = 73.0 A) and also contain a pair of molecules in the asymmetric unit. Initial results of molecular replacement calculations using the refined coordinates of the related lipase from Rhizomucor miehei identified the correct orientations and positions of the protein molecules in the unit cells of crystals of both proenzyme and the mature form.
Swenson
L
L
Medical Research Council, Canada Group in Protein Structure and Function, University of Alberta, Edmonton.
Green
R
R
Joerger
R
R
Haas
M
M
Scott
K
K
Wei
Y
Y
Derewenda
U
U
Lawson
D M
DM
Derewenda
Z S
ZS
D003460:Crystallization; D018360:Crystallography, X-Ray; D004792:Enzyme Precursors / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D012233:Rhizopus / Q000201:enzymology*
D004792:Enzyme Precursors; D008049:Lipase