Martin Jennifer L, McMillan Fiona M
Centre for Drug Design and Development, and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia.
Curr Opin Struct Biol. 2002 Dec;12(6):783-93. doi: 10.1016/s0959-440x(02)00391-3.
The S-adenosylmethionine-dependent methyltransferase enzymes share little sequence identity, but incorporate a highly conserved structural fold. Surprisingly, residues that bind the common cofactor are poorly conserved, although the binding site is localised to the same region of the fold. The substrate-binding region of the fold varies enormously. Over the past two years, there has been a significant increase in the number of structures that are known to incorporate this fold, including several uncharacterized proteins and two proteins that lack methyltransferase activity.
依赖S-腺苷甲硫氨酸的甲基转移酶在序列上几乎没有相似性，但具有高度保守的结构折叠。令人惊讶的是，结合共同辅因子的残基保守性很差，尽管结合位点位于折叠的同一区域。折叠的底物结合区域差异极大。在过去两年中，已知具有这种折叠结构的蛋白质数量显著增加，包括几种未表征的蛋白质和两种缺乏甲基转移酶活性的蛋白质。
