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The bacterial Sec protein translocase: Insights from molecular dynamics simulations

演題 The bacterial Sec protein translocase: Insights from molecular dynamics simulations
講演者 Dr.Ana-Nicoleta Bondar
Department of Physics, Freie Universität Berlin
使用言語 English
日時 2016年2月26日(金曜日) 16:00~17:00
場所 Bio Large seminar room(C109)
内容 The Sec protein translocase is an essential path for protein secretion in bacteria. In this secretion path, the soluble SecA protein motor couples hydrolysis of adenosine triphosphate (ATP) with movement of the newly synthesized protein across the membrane-embedded SecYEG protein translocon. The mechanism that ensures long-distance conformational coupling of the SecA-SecYEG protein translocase is poorly understood. To understand structural elements that help couple different regions of the Sec protein translocase, we study the all-atom molecular dynamics of SecA and SecYEG and of the SecA-SecYEG complex. We find that dynamic clusters of hydrogen bonds are essential for the conformational dynamics of SecY. The Helical Scaffold Domain (HSD) of SecA couples via hydrogen bonding to all other subunits of the protein. At the ATP-binding site of SecA, protein/water interactions in ADP-bound vs. apo SecA suggest an important functional role for a conserved carboxylate group.

問合せ先 膜分子複合機能学
塚崎智也 (ttsukaza@bs.naist.jp)

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