English Seminars
The bacterial Sec protein translocase: Insights from molecular dynamics simulations
| Title | The bacterial Sec protein translocase: Insights from molecular dynamics simulations |
| Lecturer | Dr.Ana-Nicoleta Bondar Department of Physics, Freie Universität Berlin |
| Language | English |
| Date&Time | 02/26/2016 (Fri) 16：00～17：00 |
| Venue | Bio Large seminar room(C109) |
| Detail | 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. |
| Contact | 膜分子複合機能学 塚崎智也 (ttsukaza@bs.naist.jp) |