The BAM Complex
Methods and Protocols
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Structural basis of AcrIF24 as an anti-CRISPR protein and transcriptional suppressor
Anti-CRISPR (Acr) proteins are encoded by phages to inactivate CRISPR–Cas systems of bacteria and archaea and are used to enhance the CRISPR toolbox for genome editing. Here we report the structure and mechani...
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Open AccessTdfH selectively binds metal-loaded tetrameric calprotectin for zinc import
To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). Here, we report the 6.1 Å cryoEM structure o...
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Open AccessPlasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM
In Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins is mediated by the β-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely understood....
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Structure Determination of Membrane Proteins Using X-Ray Crystallography
Membrane proteins serve essential roles in all aspects of life and make up roughly one-third of all genomes from prokaryotes to eukaryotes. Their responsibilities include mediating cell signaling, nutrient imp...
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Author Correction: A new antibiotic selectively kills Gram-negative pathogens
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
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A new antibiotic selectively kills Gram-negative pathogens
The current need for novel antibiotics is especially acute for drug-resistant Gram-negative pathogens1,2. These microorganisms have a highly restrictive permeability barrier, which limits the penetration of most ...
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The β-barrel assembly machinery in motion
In this Progress article, Buchanan and colleagues discuss recent studies that have advanced our understanding of the structure of the fully assembled β-barrel assembly machinery (BAM) complex and the interacti...
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Structural insight into the role of the Ton complex in energy transduction
In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the p...
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Summary and Future Directions
β-barrel outer membrane proteins (OMPs) are found in the outer membranes (OMs) of all gram-negative bacteria, yet exactly how they are folded and inserted remains unknown. The last decade has provided a wealth...
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Methods to Characterize Folding and Function of BamA Cross-Link Mutants
The utility of protein engineering, both the mutation and deletion of specific amino acids, to investigate protein structure and function has been demonstrated time and time again, and intermolecular and intra...
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Heat Modifiability of Outer Membrane Proteins from Gram-Negative Bacteria
β-barrel membrane proteins are somewhat unique in that their folding states can be monitored using semi-native SDS-PAGE methods to determine if they are folded properly or not. This property, which is commonly...
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Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes
In biological membranes, various protein secretion devices function as nanomachines, and measuring the internal movements of their component parts is a major technological challenge. The translocation and asse...
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Structural insight into the biogenesis of β-barrel membrane proteins
β-barrel membrane proteins are essential for nutrient import, signalling, motility and survival. In Gram-negative bacteria, the β-barrel assembly machinery (BAM) complex is responsible for the biogenesis of β-...
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Structure of the agonist-bound neurotensin receptor
Neurotensin (NTS) is a 13-amino-acid peptide that functions as both a neurotransmitter and a hormone through the activation of the neurotensin receptor NTSR1, a G-protein-coupled receptor (GPCR). In the brain,...
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Structural basis for iron piracy by pathogenic Neisseria
Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the out...
