FEBS Letters | |
Interdomain interactions within the gene 3 protein of filamentous phage | |
Riechmann, Lutz1  Hartley, Oliver2  Winter, Greg2  Griffiths, Andrew D.2  Chatellier, Jean2  Fersht, Alan R.2  | |
[1] Laboratory of Molecular Biology, MRC Centre, Hills Road, Cambridge CB2 2QH, UK;Centre for Protein Engineering, MRC Centre, Hills Road, Cambridge CB2 2QH, UK | |
关键词: Phage fd; Phage display; Protein-ligand interaction; Selection; GroEL minichaperone; g3p; gene 3 protein; D1; N-terminal domain of g3p; D2; central domain of g3p; D3; C-terminal domain of g3p; ELISA; enzyme-linked immunosorbent assay; GroEL*; minichaperone GroEL(191–345); SIP; selective infection of phage; PBS; phosphate-buffered saline; PEG; polyethylene glycol; cam; chloramphenicol; tet; tetracycline; kan; kanamycin; R; resistance; cfu; colony-forming unit; | |
DOI : 10.1016/S0014-5793(99)01658-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Infection of Escherichia coli by filamentous phage fd is mediated by the phage gene 3 protein (g3p). The g3p consists of three domains (g3p-D1, D2 and D3) linked by flexible glycine-rich linkers. All three domains are indispensable for phage infectivity; the g3p-D1 domain binds to the TolA receptor presumably at the inner face of the outer membrane, the g3p-D2 domain to the F-pilus and the g3p-D3 domain anchors g3p to the phage coat. The N-terminal domains g3p-D1 and D2 interact with each other; this interaction is abrogated by binding of g3p-D2 to the F-pilus leading to the release of g3p-D1 to bind to TolA. Here, using phages with deletions in g3p, we have discovered a specific interaction between the two N-terminal domains and g3p-D3, the C-terminal domain of g3p. We propose that these interdomain interactions within g3p lead to a compact and stable organisation when displayed on the phage tip, but that during infection, this compact state must be unraveled.
【 授权许可】
Unknown
【 预 览 】
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