Sato Dan, Yamagata Wataru, Kamei Kaeko, Nozaki Tomoyoshi, Harada Shigeharu
Department of Parasitology, Gunma University Graduate School of Medicine, 3-39-22 Showa-machi, Maebashi, Gunma 371-8511, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):1034-6. doi: 10.1107/S1744309106036694. Epub 2006 Sep 30.
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.
L-蛋氨酸γ-裂解酶（MGL）被认为是合理药物开发的一个有吸引力的靶点，因为该酶在哺乳动物宿主中不存在。为了实现基于结构的靶向MGL药物设计，两种MGL同工酶之一（EhMGL2）在正交空间群P2(1)2(1)2(1)中结晶，晶胞参数a = 88.89，b = 102.68，c = 169.87 Å。该晶体衍射分辨率为2.0 Å。不对称单元中存在四聚体（4×43.1 kDa），马修斯系数为2.2 ų Da⁻¹。该结构通过分子置换法解析，目前正在进行结构精修。
