Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly

	Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly
	Dong C(董程); Hou HF(侯海峰); Dong, C; Hou, HF; Yang, X; Shen, YQ; Dong, YH; Dong YH(董宇辉)
刊名	ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
	2012
卷号	68 期号:2 页码:95-101
关键词	Gram-negative bacteria BAM complex OMP POTRA domains TPR motif
英文摘要	The outer membrane protein complex (BAM complex) plays an important role in outer membrane protein (OMP) assembly in Escherichia coli. The BAM complex includes the integral beta-barrel protein BamA as well as four lipoproteins: BamB, BamC, BamD and BamE. One of these lipoproteins, BamD, is similar to essential for the survival of Escherichia coli. The structure of BamD at 2.6 angstrom resolution shows that this lipoprotein is composed of ten a-helices that form five tetratricopeptide-repeat (TPR) motifs. The arrangement of the BamD motifs is similar to that in the periplasmic part of BamA. One of the ten a-helices, a10, which has been shown to be important for the similar to assembly of the BAM complex, is located in the very C-terminal region of BamD. A deep groove between TPR domains 4 and 5 is also observed. This groove, as well as the surface around a10, may provide binding sites for other components of the BAM complex. The C-terminal region of similar to BamD serves as a platform for interactions with other components of the BAM complex. The N-terminal region shares structural similarity to other proteins whose functions are related to assistance in or regulation of secretion. Therefore, this region is likely to play an important role in the insertion of other outer membrane proteins.
学科主题	Biochemistry & Molecular Biology; Biophysics; Crystallography
收录类别	SCI
WOS记录号	WOS:000299469100001
公开日期	2016-05-03
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/223838]
专题	中国科学院高能物理研究所
推荐引用方式 GB/T 7714	Dong C,Hou HF,Dong, C,et al. Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly[J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,2012,68(2):95-101.
APA	董程.,侯海峰.,Dong, C.,Hou, HF.,Yang, X.,...&董宇辉.(2012).Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly.ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,68(2),95-101.
MLA	董程,et al."Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly".ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 68.2(2012):95-101.