Huang Lan, Hung Liwei, Odell Mark, Yokota Hisao, Kim Rosalind, Kim Sung-Hou
Dept. of Cellular Biochemistry and Biophysics, Sloan Kettering Institute, 1275 York Ave., New York, NY 10021, USA.
J Struct Funct Genomics. 2002;2(3):121-7. doi: 10.1023/a:1021279113558.
We have determined the three-dimensional (3-D) structure of protein MJ0882, which derives from a hypothetical open reading frame in the genome of the hyperthermophile Methanococcus jannaschii. The 3-D fold of MJ0882 at 1.8 A highly resembles that of a methyltransferase, despite limited sequence similarity to any confirmed methyltransferase. The structure has an S-adenosylmethionine (AdoMet) binding pocket surrounded by motifs with similarities to those commonly found among AdoMet binding proteins. Preliminary biochemical experiments show that MJ0882 specifically binds to AdoMet, which is the essential co-factor for methyltransferases.
我们已经确定了蛋白质MJ0882的三维（3-D）结构，该蛋白质源自嗜热古菌詹氏甲烷球菌基因组中的一个假设开放阅读框。尽管与任何已确认的甲基转移酶的序列相似性有限，但MJ0882在1.8埃分辨率下的三维折叠结构与甲基转移酶的结构高度相似。该结构有一个S-腺苷甲硫氨酸（AdoMet）结合口袋，其周围的基序与AdoMet结合蛋白中常见的基序相似。初步生化实验表明，MJ0882特异性结合AdoMet，而AdoMet是甲基转移酶的必需辅因子。
