TERNARY STRUCTURE OF CYTOCHROME P450BM 3 HEME DOMAIN CO COMPLEX

细胞色素P450 BM-3血红素结构域与底物的2.7E数据集 1996年5月在SSRL收集了一个结合，并解决了结构 分子置换。 这个结构揭示了一个巨大的 底物结合时蛋白质骨架的构象变化 这导致衬底进入通道的关闭。 我们 进一步筛选出较好的低温保护剂， 条件下，也将试图通过交联稳定晶体与 戊二醛 三元晶体结构的测定 P450 BM-3血红素结构域-底物-CO复合物可能是 将血红素锁定在其亚铁态，由此可能的底物 可以检测到构象变化。

A 2.7 E data set of cytochrome P450BM-3 heme domain with substrate bound was collected in May, 1996 at SSRL and the structure was solved by molecular replacement. This structure reveals a large conformational change in protein backbone upon the substrate binding which results in the closure of the substrate access channel. We are going to further screen better cryo-protectant and reducing conditions, also will try to stabilize crystals by cross linking with glutaraldehyde. Determination of a ternary crystal structure of P450BM-3 heme domain-substrate-CO complex might be the only way to lock the heme in its ferrous state from which the possible substrate conformational changes can be detected.