Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA
文献类型:期刊论文
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作者 | Chen Z(陈真); Zhan LH(詹利红); Hou HF(侯海峰)![]() ![]() ![]() ![]() |
刊名 | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
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出版日期 | 2016 ; 2016 |
卷号 | 72期号:2页码:236-244 |
关键词 | outer membrane proteins BamB POTRA domains assembly and insertion crystal structure outer membrane proteins BamB POTRA domains assembly and insertion crystal structure |
ISSN号 | 2059-7983 |
DOI | 10.1107/S2059798315024729 ; 10.1107/S2059798315024729 |
通讯作者 | 董城 ; 董宇辉 ; 董城 ; 董宇辉 |
文献子类 | 期刊论文 ; Article |
英文摘要 | In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAMcomplex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 angstrom resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain.; In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAMcomplex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 angstrom resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain. |
WOS关键词 | BARREL ASSEMBLY MACHINERY ; OUTER-MEMBRANE PROTEINS ; ESCHERICHIA-COLI BAMB ; CRYSTAL-STRUCTURE ; ESSENTIAL COMPONENT ; PERIPLASMIC DOMAIN ; YAET COMPLEX ; BIOGENESIS ; ROLES ; FLEXIBILITY ; BARREL ASSEMBLY MACHINERY ; OUTER-MEMBRANE PROTEINS ; ESCHERICHIA-COLI BAMB ; CRYSTAL-STRUCTURE ; ESSENTIAL COMPONENT ; PERIPLASMIC DOMAIN ; YAET COMPLEX ; BIOGENESIS ; ROLES ; FLEXIBILITY |
语种 | 英语 ; 英语 |
WOS记录号 | WOS:000373718400006 ; WOS:000373718400006 |
源URL | [http://ir.ihep.ac.cn/handle/311005/260430] ![]() |
专题 | 高能物理研究所_多学科研究中心 |
作者单位 | 中国科学院高能物理研究所 |
推荐引用方式 GB/T 7714 | Chen Z,Zhan LH,Hou HF,et al. Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA, Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA[J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,2016, 2016,72, 72(2):236-244, 236-244. |
APA | 陈真.,詹利红.,侯海峰.,高增强.,徐建华.,...&Dong, YH.(2016).Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA.ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,72(2),236-244. |
MLA | 陈真,et al."Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA".ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72.2(2016):236-244. |
入库方式: OAI收割
来源:高能物理研究所
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