Wigley D B, Davies G J, Dodson E J, Maxwell A, Dodson G
Department of Chemistry, York University, Heslington, UK.
Nature. 1991 Jun 20;351(6328):624-9. doi: 10.1038/351624a0.
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 A resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 A hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.
已解析出与一种不可水解的ATP类似物复合的大肠杆菌DNA促旋酶B蛋白N端片段的晶体结构，分辨率为2.5埃。它由两个结构域组成，二者均含有新颖的蛋白质折叠。该蛋白质片段形成二聚体，其N端结构域负责ATP结合与水解。C端结构域构成穿过蛋白质二聚体的一个20埃孔洞的侧面，这可能在超螺旋反应期间的DNA链通过过程中发挥作用。
