枯草芽孢杆菌双精氨酸转运系统TatAy 蛋白的溶液结构
收稿日期: 2015-02-09
修回日期: 2015-05-09
网络出版日期: 2015-06-05
基金资助
Grant from the Ministry of Science and Technology of China (2010IM030700) and the National Natural Science Foundation of China (31070649).
Solution Structure of Bacillus subtilis Twin-Arginine Translocation TatAy Protein
Received date: 2015-02-09
Revised date: 2015-05-09
Online published: 2015-06-05
Supported by
Grant from the Ministry of Science and Technology of China (2010IM030700) and the National Natural Science Foundation of China (31070649).
存在于细菌和植物叶绿体中的双精氨酸(Tat)蛋白质转运系统能将底物蛋白以折叠的状态进行跨膜转运．该系统中的单次跨膜膜蛋白TatA 通过自身寡聚形成转运
底物蛋白的通道．该文应用液体核磁共振方法解析了枯草芽孢杆菌TatAy 蛋白在十二烷基胆碱磷酸胶束中的结构，它是由一个跨膜螺旋(TMH)和一个两亲性螺旋(APH)构成的L 型结构．通过与已经报道的枯草芽孢杆菌TatAd 蛋白的结构比较，该文能够鉴定出参与维持L 型构象的重要氨基酸残基，并指出了TatA 蛋白家族中若干较为保守的结构特征．在此基础上，该文讨论了保守残基在TatA 通道形成过程中可能发挥的作用．
胡蕴菲1,2，何鹏1,3，吴宇杰1,3，金长文1,2,3,4* . 枯草芽孢杆菌双精氨酸转运系统TatAy 蛋白的溶液结构[J]. 波谱学杂志, 2015 , 32(2) : 291 -307 . DOI: 10.11938/cjmr20150212
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.
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