Literature DB >> 26621472

Structural Aspects of Bacterial Outer Membrane Protein Assembly.

Charles Calmettes1, Andrew Judd2, Trevor F Moraes3.   

Abstract

The outer membrane of Gram-negative bacteria is predominantly populated by β-Barrel proteins and lipid anchored proteins that serve a variety of biological functions. The proper folding and assembly of these proteins is essential for bacterial viability and often plays a critical role in virulence and pathogenesis. The β-barrel assembly machinery (Bam) complex is responsible for the proper assembly of β-barrels into the outer membrane of Gram-negative bacteria, whereas the localization of lipoproteins (Lol) system is required for proper targeting of lipoproteins to the outer membrane.

Entities:  

Keywords:  Bam machinery; Lol pathway; Omp85 family; Outer membrane biogenesis; Protein trafficking

Mesh:

Substances:

Year:  2015        PMID: 26621472     DOI: 10.1007/978-3-319-23603-2_14

Source DB:  PubMed          Journal:  Adv Exp Med Biol        ISSN: 0065-2598            Impact factor:   2.622


  3 in total

1.  Impact of Moderate Temperature Changes on Neisseria meningitidis Adhesion Phenotypes and Proteome.

Authors:  Martin Lappann; Andreas Otto; Madita Brauer; Dörte Becher; Ulrich Vogel; Kay Johswich
Journal:  Infect Immun       Date:  2016-11-18       Impact factor: 3.441

2.  Detecting Lipoproteins Sneaking Out of the Lipopolysaccharide Leaflet.

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

3.  An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.

Authors:  Marcin Michalik; Marcella Orwick-Rydmark; Michael Habeck; Vikram Alva; Thomas Arnold; Dirk Linke
Journal:  PLoS One       Date:  2017-08-03       Impact factor: 3.240

  3 in total

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