Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex.

@article{Kim2011StructuralCO,
  title={Structural characterization of Escherichia coli BamE, a lipoprotein component of the $\beta$-barrel assembly machinery complex.},
  author={Kelly H. Kim and Hyun-Seo Kang and Mark Okon and Eric Escobar-Cabrera and Lawrence P. McIntosh and Mark Paetzel},
  journal={Biochemistry},
  year={2011},
  volume={50 6},
  pages={
          1081-90
        }
}
In Escherichia coli, the BAM complex catalyzes the essential process of assembling outer membrane proteins (OMPs). This complex consists of five proteins: one membrane-bound protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Despite their importance in OMP biogenesis, there is currently a lack of functional and structural information on the BAM complex lipoproteins. BamE is the smallest but most conserved lipoprotein in the complex. The structural and dynamic properties of… 
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Results suggest that an identified surface on the C-terminal domain of BamC may serve as an important protein-binding surface for interaction with other BAM-complex components or substrates.
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In Escherichia coli, a multicomponent BAM (β-barrel assembly machinery) complex is responsible for recognition and assembly of outer membrane β-barrel proteins. The functionality of BAM in protein…
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TLDR
A mechanism of OMP biogenesis in which substrates are partially folded inside the barrel cavity and are subsequently released laterally into the lipid bilayer is strongly supported.
Crystal Structure of β-Barrel Assembly Machinery BamCD Protein Complex*
TLDR
The first crystal structure of a Bam lipoprotein complex is reported, showing how BamC and BamD interact and suggesting that this region of BamC may play a regulatory role in outer membrane protein biogenesis.
Crystal structure of BamD: an essential component of the β-Barrel assembly machinery of gram-negative bacteria.
Structure Determination of the BAM Complex Accessory Lipoproteins BamB-E.
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    Methods in molecular biology
  • 2015
TLDR
Structures of BamB to BamE have been determined using X-ray crystallography, NMR and SAXS techniques, and a brief summary of the currently available structural Bam protein repertoire is given.
BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.
TLDR
Findings indicate that the unique β16C strand and the periplasmic turns of BamA are important for the outer membrane insertion and assembly, which is important for understanding the OMP insertion in Gram-negative bacteria, as well as in mitochondria and chloroplasts.
Structural basis of outer membrane protein insertion by the BAM complex
TLDR
The authors' structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB–BamE, in the periplasm, and indicate that these subunits rotate with respect to the integral membrane β-barrel of Bam a to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP.
NMR studies of the BamA complex proteins at high resolution
The β-barrel assembly machinery (BAM) complex is essential for the biogenesis of outer membrane proteins (OMPs) in Gram-negative bacteria, with the membrane protein BamA acting as a catalyst for…
Plasticity of the β-barrel assembly machinery investigated by NMR
TLDR
This thesis described ssNMR studies on the dynamics of BamA and its interactions with the lipid bilayer and the lipoproteins BamCDE and introduced a new approach termed “proton-clouds”, in which fully protonated amino acids are incorporated in a deuterated background.
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