Abstract
L-Methionine gamma-lyase (MGL) is a pyridoxal phosphate-dependent enzyme that is involved in the degradation of sulfur-containing amino acids. MGL is an attractive drug target against amoebiasis because the mammalian host of its causative agent Entamoeba histolytica lacks MGL. For the development of anti-amoebic agents based on the structure of MGL, one of two MGL isoenzymes (EhMGL1) was crystallized in the monoclinic space group P2(1), with unit-cell parameters a = 99.12, b = 85.38, c = 115.37 A, beta = 101.82 degrees . The crystals diffract to beyond 2.0 A resolution. The presence of a tetramer in the asymmetric unit (4 x 42.4 kDa) gives a Matthews coefficient of 2.8 A(3) Da(-1) and a solvent content of 56%. The structure was solved by the molecular-replacement method and structure refinement is now in progress.