Literature DB >> 27862971

Structural snapshots of the β-barrel assembly machinery.

Jeremy Bakelar1, Susan K Buchanan2, Nicholas Noinaj1.   

Abstract

The β-barrel assembly machinery (BAM) is a multicomponent complex responsible for the biogenesis of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria, with conserved systems in both mitochondria and chloroplasts. Given its importance in the integrity of the outer membrane and in the assembly of surface exposed virulence factors, BAM is an attractive therapeutic target against pathogenic bacteria, particularly multidrug-resistant strains. While the mechanism for how BAM functions remains elusive, previous structural studies have described each of the individual components of BAM, offering only a few clues to how the complex functions. Recently, a number of structures have been reported of complexes, including that of fully assembled BAM in differing conformational states. These studies have provided the molecular blueprint detailing the atomic interactions between the components and have revealed new details about BAM, which suggest a dynamic mechanism that may use conformational changes to assist in the biogenesis of new OMPs. © Published 2016. This article is a U.S. Government work and is in the public domain in the USA.

Entities:  

Keywords:  BAM complex; MD simulations; X-ray crystallography; lateral gate; membrane biogenesis; membrane protein; outer membrane protein; protein folding; β-barrel assembly machinery; β-barrel membrane proteins

Mesh:

Substances:

Year:  2016        PMID: 27862971      PMCID: PMC5429997          DOI: 10.1111/febs.13960

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  55 in total

1.  Activation of the Escherichia coli β-barrel assembly machine (Bam) is required for essential components to interact properly with substrate.

Authors:  Dante P Ricci; Christine L Hagan; Daniel Kahne; Thomas J Silhavy
Journal:  Proc Natl Acad Sci U S A       Date:  2012-02-13       Impact factor: 11.205

2.  Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli.

Authors:  Tao Wu; Andrew C McCandlish; Luisa S Gronenberg; Shu-Sin Chng; Thomas J Silhavy; Daniel Kahne
Journal:  Proc Natl Acad Sci U S A       Date:  2006-07-21       Impact factor: 11.205

3.  Inhibition of the β-barrel assembly machine by a peptide that binds BamD.

Authors:  Christine L Hagan; Joseph S Wzorek; Daniel Kahne
Journal:  Proc Natl Acad Sci U S A       Date:  2015-02-02       Impact factor: 11.205

4.  Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli.

Authors:  Drew Bennion; Emily S Charlson; Eric Coon; Rajeev Misra
Journal:  Mol Microbiol       Date:  2010-09       Impact factor: 3.501

Review 5.  The Bam machine: a molecular cooper.

Authors:  Dante P Ricci; Thomas J Silhavy
Journal:  Biochim Biophys Acta       Date:  2011-08-22

6.  Crystal structure of YaeT: conformational flexibility and substrate recognition.

Authors:  Petia Z Gatzeva-Topalova; Troy A Walton; Marcelo C Sousa
Journal:  Structure       Date:  2008-12-10       Impact factor: 5.006

7.  Structure of BamA, an essential factor in outer membrane protein biogenesis.

Authors:  Reinhard Albrecht; Monika Schütz; Philipp Oberhettinger; Michaela Faulstich; Ivan Bermejo; Thomas Rudel; Kay Diederichs; Kornelius Zeth
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2014-05-30

8.  Structural insight into the biogenesis of β-barrel membrane proteins.

Authors:  Nicholas Noinaj; Adam J Kuszak; James C Gumbart; Petra Lukacik; Hoshing Chang; Nicole C Easley; Trevor Lithgow; Susan K Buchanan
Journal:  Nature       Date:  2013-09-01       Impact factor: 49.962

9.  Reconstitution of bacterial autotransporter assembly using purified components.

Authors:  Giselle Roman-Hernandez; Janine H Peterson; Harris D Bernstein
Journal:  Elife       Date:  2014-09-02       Impact factor: 8.140

10.  Crystal structure of BamB from Pseudomonas aeruginosa and functional evaluation of its conserved structural features.

Authors:  Katarina Bartoš Jansen; Susan Lynn Baker; Marcelo Carlos Sousa
Journal:  PLoS One       Date:  2012-11-26       Impact factor: 3.240

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  4 in total

1.  Interfering with outer membrane biogenesis to fight Gram-negative bacterial pathogens.

Authors:  Raffaele Ieva
Journal:  Virulence       Date:  2017-02-17       Impact factor: 5.882

Review 2.  Tools for the Recognition of Sorting Signals and the Prediction of Subcellular Localization of Proteins From Their Amino Acid Sequences.

Authors:  Kenichiro Imai; Kenta Nakai
Journal:  Front Genet       Date:  2020-11-25       Impact factor: 4.599

3.  Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.

Authors:  Cecilia Pinto; Deni Mance; Tessa Sinnige; Mark Daniëls; Markus Weingarth; Marc Baldus
Journal:  Nat Commun       Date:  2018-10-08       Impact factor: 14.919

4.  Comparative Analysis of TM and Cytoplasmic β-barrel Conformations Using Joint Descriptor.

Authors:  Jayaraman Thangappan; Sangwook Wu; Sun-Gu Lee
Journal:  Sci Rep       Date:  2018-09-21       Impact factor: 4.379

  4 in total

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