Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.

@article{Vassylyev2006CrystalSO,
  title={Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.},
  author={Dmitry G. Vassylyev and Hiroyuki Mori and Marina N. Vassylyeva and Tomoya Tsukazaki and Yoshiaki Kimura and Tahir H. Tahirov and Koreaki Ito},
  journal={Journal of molecular biology},
  year={2006},
  volume={364 3},
  pages={248-58}
}
The mechanism of pre-protein export through the bacterial cytoplasmic membrane, in which the SecA ATPase plays a crucial role as an "energy supplier", is poorly understood. In particular, biochemical and structural studies provide contradictory data as to the oligomeric state of SecA when it is integrated into the active trans-membrane translocase. Here, we report the 2.8 A resolution crystal structure of the Thermus thermophilus SecA protein (TtSecA). Whereas the structure of the TtSecA… CONTINUE READING