中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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); Gao ZQ(高增强); Xu JH(徐建华); Dong C(董城); Dong YH(董宇辉); Chen, Z; Zhan, LH; Hou, HF
刊名ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY ; ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
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
DOI10.1107/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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