Expression, purification and crystallization of L-methionine gamma-lyase 2 from Entamoeba histolytica.
L-Methionine gamma-lyase (MGL) is considered to be an attractive target for rational drug development because the enzyme is absent in mammalian hosts. To enable structure-based design of drugs targeting MGL, one of the two MGL isoenzymes (EhMGL2) was crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 88.89, b = 102.68, c = 169.87 A. The crystal diffracted to a resolution of 2.0 A. The presence of a tetramer in the asymmetric unit (4 x 43.1 kDa) gives a Matthews coefficient of 2.2 A(3) Da(-1). The structure was solved by the molecular-replacement method and structure refinement is now in progress.
Sato
Dan
D
Department of Parasitology, Gunma University Graduate School of Medicine, 3-39-22 Showa-machi, Maebashi, Gunma 371-8511, Japan.
Yamagata
Wataru
W
Kamei
Kaeko
K
Nozaki
Tomoyoshi
T
Harada
Shigeharu
S
D000818:Animals; D013437:Carbon-Sulfur Lyases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D004748:Entamoeba histolytica / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction
D007527:Isoenzymes; D011994:Recombinant Proteins; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase