Subramanya H S, Doherty A J, Ashford S R, Wigley D B
Laboratory of Molecular Biophysics, University of Oxford, United Kingdom.
Cell. 1996 May 17;85(4):607-15. doi: 10.1016/s0092-8674(00)81260-x.
The crystal structure of the ATP-dependent DNA ligase from bacteriophage T7 has been solved at 2.6 A resolution. The protein comprises two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotide binding pocket is situated on the larger N-terminal domain, at the base of the cleft between the two domains of the enzyme. Comparison of the overall domain structure with that of DNA methyltransferases, coupled with other evidence, suggests that DNA also binds in this cleft. Since this structure is the first of the nucleotidyltransferase superfamily, which includes the eukaryotic mRNA capping enzymes, the relationship between the structure of DNA ligase and that of other nucleotidyltransferases is also discussed.
噬菌体T7的ATP依赖性DNA连接酶的晶体结构已在2.6埃分辨率下解析出来。该蛋白质由两个结构域组成,它们之间有一条深裂缝。与ATP形成的复合物的结构表明,核苷酸结合口袋位于较大的N端结构域上,在酶的两个结构域之间裂缝的底部。将整体结构域结构与DNA甲基转移酶的结构域结构进行比较,并结合其他证据表明,DNA也结合在这个裂缝中。由于这种结构是核苷酸转移酶超家族中的首个结构,该超家族包括真核mRNA加帽酶,因此还讨论了DNA连接酶的结构与其他核苷酸转移酶结构之间的关系。