Chinese Journal of Magnetic Resonance ›› 2015, Vol. 32 ›› Issue (2): 291-307.doi: 10.11938/cjmr20150212

Previous Articles     Next Articles

Solution Structure of Bacillus subtilis Twin-Arginine Translocation TatAy Protein

HU Yun-fei1,2,HE Peng3,WU Yu-jie1,3,JIN Chang-wen1,2,3,4*   

  1. 1. Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871;
    2. College of Chemistry and Molecular Engineering, Peking University, Beijing 100871;
    3. College of Life Sciences, Peking University, Beijing 100871;
    4. Beijing National Laboratory for Molecular Sciences, Peking University, Beijing 100871
  • Received:2015-02-09 Revised:2015-05-09 Online:2015-06-05 Published:2015-06-05
  • About author:HU Yun-fei(1983-), female, born in Fujian, PhD., her research focuses on NMR spectroscopy of biological macromolecules. *Corresponding author: JIN Chang-wen, Tel: +86-10-62756004, E-mail: changwen@pku.edu.cn.
  • Supported by:

    Grant from the Ministry of Science and Technology of China (2010IM030700) and the National Natural Science Foundation of China (31070649).

Abstract:

The twin-arginine transport (Tat) systems in bacteria and plant chloroplasts translocate cargo proteins across cellular membranes in their folded states. The single-pass transmembrane protein TatA forms the protein translocation channel via self-oligomerization. Herein, we present the structure of Bacillus subtilis TatAy protein in dodecylphosphocholine micelles determined by solution NMR method. TatAy adopts an L-shaped conformation formed by a transmembrane helix (TMH) and an amphipathic helix (APH). Structural comparison of TatAy protein with the previously reported B. subtilis TatAd protein highlights essential residues at the hinge region for maintaining the L-shaped conformation, and suggests a few conserved structural features for the
TatA protein family. Possible roles for the conserved residues in the TatA channel formation are discussed.

Key words: twin-arginine translocation, membrane protein, protein structure, solution NMR

CLC Number: