Solution structure of the TatB component of the twin-arginine   translocation system

doi:10.1016/j.bbamem.2014.03.015

CORC > 北京大学 > 化学与分子工程学院

	Solution structure of the TatB component of the twin-arginine translocation system
	Zhang, Yi ; Wang, Lei ; Hu, Yunfei ; Jin, Changwen
刊名	biochimica et biophysica acta biomembranes
	2014
关键词	Protein transport Twin-arginine translocation (Tat) Membrane protein Protein structure Protein dynamics NMR PROTEIN-TRANSPORT SYSTEM ESCHERICHIA-COLI TATA PRECURSOR PROTEINS BACKBONE DYNAMICS DIPOLAR COUPLINGS NMR-SPECTROSCOPY SIGNAL PEPTIDES PATHWAY BINDING DOMAIN
DOI	10.1016/j.bbamem.2014.03.015
英文摘要	The twin-arginine protein transport (Tat) system translocates fully folded proteins across lipid membranes. In Escherichia coli, the Tat system comprises three essential components: TatA, TatB and TatC The protein translocation process is proposed to initiate by signal peptide recognition and substrate binding to the TatBC complex. Upon formation of the TatBC-substrate protein complex, the TatA subunits are recruited and form the protein translocation pore. Experimental evidences suggest that TatB forms a tight complex with TatC at 1:1 molar ratio and the TatBC complex contains multiple copies of both proteins. Cross-linking experiments demonstrate that TatB functions in tetrameric units and interacts with both TatC and substrate proteins. However, structural information of the TatB protein is still lacking, and its functional mechanism remains elusive. Herein, we report the solution structure of TatB in DPC micelles determined by Nuclear Magnetic Resonance (NMR) spectroscopy. Overall, the structure shows an extended 'L-shape' conformation comprising four helices: a transmembrane helix (TMH) alpha 1, an amphipathic helix (APH)alpha 2, and two solvent exposed helices alpha 3 and alpha 4. The packing of TMH and APH is relatively rigid, whereas helices alpha 3 and alpha 4 display notably higher mobility. The observed floppiness of helices alpha 3 and alpha 4 allows TatB to sample a large conformational space, thus providing high structural plasticity to interact with substrate proteins of different sizes and shapes. (C) 2014 Elsevier B.V. All rights reserved.; Biochemistry & Molecular Biology; Biophysics; SCI(E); PubMed; 4; ARTICLE; yunfei@pku.edu.cn; changwen@pku.edu.cn; 7; 1881-1888; 1838
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/162449]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Zhang, Yi,Wang, Lei,Hu, Yunfei,et al. Solution structure of the TatB component of the twin-arginine translocation system[J]. biochimica et biophysica acta biomembranes,2014.
APA	Zhang, Yi,Wang, Lei,Hu, Yunfei,&Jin, Changwen.(2014).Solution structure of the TatB component of the twin-arginine translocation system.biochimica et biophysica acta biomembranes.
MLA	Zhang, Yi,et al."Solution structure of the TatB component of the twin-arginine translocation system".biochimica et biophysica acta biomembranes (2014).