Crystal structure of the replication terminator protein from B. subtilis at 2.6 A.
Crystal structure of the replication terminator protein from B. subtilis at 2.6 A.
复制标题
枯草芽孢杆菌复制终止子蛋白的晶体结构，2.6 A。
DOI：
10.1016/0092-8674(95)90519-7
复制
发表时间：
1995
期刊：
影响因子：
64.5
通讯作者：
White,SW
中科院分区：
文献类型：
--
作者：
Bussiere,DE;Bastia,D;White,SW
B的复制终止蛋白（RTP）的晶体结构。枯草芽孢杆菌已被确定为2.6。一项决议。如先前通过生物化学和生物物理学研究所表明的，该分子作为对称二聚体存在，并且处于α + J~蛋白质折叠类。该蛋白具有几个不常见的特征，包括作为二聚化结构域的反平行卷曲螺旋，以及适合与B-DNA的大沟和小沟相互作用的α-螺旋和I-带。一个网站已被确定在RTP的表面上，是生化和位置适合与replicationspecific解旋酶的相互作用。结构的其他特征与蛋白质的极性逆解旋酶机制一致。提出了RTP与同源DNA相互作用的模型。
The crystal structure of the replication terminator protein (RTP) of B. subtilis has been determined at 2.6. A resolution. As previously suggested by both biochemical and biophysical studies, the molecule exists as a symmetric dimer and is in the a+ J~ protein-folding class. The protein has several uncommon features, including an antiparallel coiled-coil, which serves as the dimerization domain, and both an a-helix and a I~-ribbon suitably positioned to interact with the major and minor grooves of B-DNA. A site has been identified on the surface of RTP that is biochemically and positionally suitable for interaction with the replicationspecific helicase. Other features of the structure are consistent with the polar contrahelicase mechanism of the protein. A model of the interaction between RTP and its cognate DNA is presented.