Literature DB >> 26427688

Identification of BamC on the Surface of E. coli.

Chaille T Webb1, Trevor Lithgow2.   

Abstract

In order to relate the structural architecture of the BAM complex to its function in outer membrane protein assembly, the arrangement of each component within the complex is vital. This chapter explores the structure and topology of BamC, using a range of biochemical techniques to probe the topology and surface exposure.

Entities:  

Keywords:  Immunofluorescence; Lipoprotein; Outer membrane; Surface exposure; Topology

Mesh：

Substances：

Year:  2015        PMID： 26427688     DOI： 10.1007/978-1-4939-2871-2_17

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


  3 in total

1.  Disorder is a critical component of lipoprotein sorting in Gram-negative bacteria.

Authors:  Jessica El Rayes; Joanna Szewczyk; Michaël Deghelt; Naemi Csoma; André Matagne; Bogdan I Iorga; Seung-Hyun Cho; Jean-François Collet
Journal:  Nat Chem Biol       Date:  2021-07-29       Impact factor: 15.040

2.  Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli.

Authors:  L E Petrovskaya; A V Zlobinov; L N Shingarova; E F Boldyreva; S Sh Gapizov; K A Novototskaya-Vlasova; E M Rivkina; D A Dolgikh; M P Kirpichnikov
Journal:  Extremophiles       Date:  2017-12-18       Impact factor: 2.395

3.  Detecting Lipoproteins Sneaking Out of the Lipopolysaccharide Leaflet.

Authors:  Naemi Csoma; Didier Colau; Jean-François Collet
Journal:  Methods Mol Biol       Date:  2022
  3 in total

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