Literature DB >> 11255120

Expression and properties of bacteriophage T4 gene product 11.

L P Kurochkina1, P G Leiman, S Y Venyaminov, V V Mesyanzhinov.   

Abstract

A plasmid vector for expression of bacteriophage T4 gene product 11 (gp11) in E. coli cells has been constructed. Gp11 is a baseplate protein that connects short tail fibers providing irreversible adsorption of the virus on a cell. A method based on chromatography on hydroxyapatite has been developed for purification of recombinant gp11. The protein is active in an in vitro complementation assay and transforms defective phage particles lacking gp11 into infective ones. Gel filtration data suggest that the biologically active protein is a trimer. According to CD spectroscopy and sequence analysis data, the polypeptide chain of gp11 contains not less than 20% alpha-helical segments, about 30% beta-structure, and belongs to the class of alpha/beta structural proteins.

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Year:  2001        PMID: 11255120     DOI: 10.1023/a:1002831212462

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  2 in total

Review 1.  Homotrimeric, beta-stranded viral adhesins and tail proteins.

Authors:  Peter R Weigele; Eben Scanlon; Jonathan King
Journal:  J Bacteriol       Date:  2003-07       Impact factor: 3.490

2.  Trimeric autotransporters require trimerization of the passenger domain for stability and adhesive activity.

Authors:  Shane E Cotter; Neeraj K Surana; Susan Grass; Joseph W St Geme
Journal:  J Bacteriol       Date:  2006-08       Impact factor: 3.490

  2 in total

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