Sato Dan, Karaki Tsuyoshi, Shimizu Akira, Kamei Kaeko, Harada Shigeharu, Nozaki Tomoyoshi
Institute for Advanced Biosciences, Keio University, 246-2 Mizukami, Kakuganji, Tsuruoka, Yamagata 997-0052, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):697-9. doi: 10.1107/S1744309108018691. Epub 2008 Jul 5.
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.
L-蛋氨酸γ-裂合酶（MGL）是一种依赖磷酸吡哆醛的酶，参与含硫氨基酸的降解。MGL是抗阿米巴病的一个有吸引力的药物靶点，因为其病原体溶组织内阿米巴的哺乳动物宿主缺乏MGL。为了基于MGL的结构开发抗阿米巴药物，两种MGL同工酶之一（EhMGL1）在单斜空间群P2(1)中结晶，晶胞参数为a = 99.12、b = 85.38、c = 115.37 Å，β = 101.82°。这些晶体的衍射分辨率超过2.0 Å。不对称单元中存在四聚体（4×42.4 kDa），马修斯系数为2.8 ų Da⁻¹，溶剂含量为56%。该结构通过分子置换法解析，目前正在进行结构精修。
