Literature DB >> 3582670

Conformation of colicin A: apparent difference between cytoplasmic and extracellular polypeptide chain.

M Knibiehler, C Lazdunski.   

Abstract

Cytoplasmic colicin A has the ability to bind to membranes and to form stable dimers. This form remains stable even in the presence of 1% SDS at 25 degrees C. Both of these properties were not observed for extracellular colicin A suggesting a possible difference in the conformation between cytoplasmic and extracellular colicin A.

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Year:  1987        PMID: 3582670     DOI: 10.1016/0014-5793(87)80686-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Colicin cleavage by OmpT protease during both entry into and release from Escherichia coli cells.

Authors:  D Cavard; C Lazdunski
Journal:  J Bacteriol       Date:  1990-02       Impact factor: 3.490

2.  Assembly of colicin A in the outer membrane of producing Escherichia coli cells requires both phospholipase A and one porin, but phospholipase A is sufficient for secretion.

Authors:  Daniele Cavard
Journal:  J Bacteriol       Date:  2002-07       Impact factor: 3.490

3.  Synthesis and functioning of the colicin E1 lysis protein: comparison with the colicin A lysis protein.

Authors:  D Cavard
Journal:  J Bacteriol       Date:  1991-01       Impact factor: 3.490

4.  The glucuronyltransferase GlcAT-P is required for stretch growth of peripheral nerves in Drosophila.

Authors:  Rahul Pandey; Jorge Blanco; Gerald Udolph
Journal:  PLoS One       Date:  2011-11-23       Impact factor: 3.240

  4 in total

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