Renwick S B, Skelly J V, Chave K J, Sanders P G, Snell K, Baumann U
Section of Structural Biology, Institute of Cancer Research, University of London, Cotswold Road, Sutton, Surrey SM2 5NG, England.
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1030-1. doi: 10.1107/s0907444998004272.
As an enzyme of the thymidylate synthase cycle, serine hydroxymethyltransferase (SHMT) has a key role in nucleotide biosynthesis. Elevated activities of SHMT have been correlated with the increased demand for nucleotide biosynthesis in tumors of human and rodent origin, making this enzyme a novel target for cancer chemotherapy. Here the purification and crystallization of recombinant human cytosolic SHMT are reported. Crystals belong to space group P6222 or P6422 with cell parameters a = b = 155.0, c = 235.5 A and diffract to at least 3.0 A resolution.
作为胸苷酸合酶循环中的一种酶，丝氨酸羟甲基转移酶（SHMT）在核苷酸生物合成中起关键作用。SHMT活性升高与人和啮齿动物来源肿瘤中核苷酸生物合成需求增加相关，这使得该酶成为癌症化疗的新靶点。本文报道了重组人胞质SHMT的纯化及结晶过程。晶体属于空间群P6222或P6422，晶胞参数a = b = 155.0，c = 235.5 Å，衍射分辨率至少为3.0 Å。
