Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly
文献类型：期刊论文
| 作者 | Dong C(董程); Hou HF(侯海峰) ; Dong, C; Hou, HF; Yang, X; Shen, YQ; Dong, YH; Dong YH(董宇辉)
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| 刊名 | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
 |
| 出版日期 | 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 |
| 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. |
入库方式： OAI收割
来源：高能物理研究所
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