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Related Concept Videos

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Related Experiment Video

Updated: May 22, 2026

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

The bacterial outer membrane β-barrel assembly machinery.

Kelly H Kim1, Suraaj Aulakh, Mark Paetzel

  • 1Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada.

Protein Science : a Publication of the Protein Society
|May 3, 2012
PubMed
Summary

The bacterial β-barrel assembly machinery (BAM) complex is crucial for outer membrane protein assembly in Gram-negative bacteria. This review details recent advances in understanding BAM complex structure and function, vital for bacterial viability and virulence.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Outer membrane proteins, specifically β-barrels, are essential for Gram-negative bacteria.
  • The correct folding and assembly of these proteins are critical for bacterial survival and can influence pathogenicity.
  • The β-barrel assembly machinery (BAM) complex facilitates the insertion of β-barrel proteins into the bacterial outer membrane.

Purpose of the Study:

  • To review and summarize recent significant advancements in the understanding of the bacterial BAM complex.
  • To consolidate current knowledge on the structure and function of the BAM complex.

Main Methods:

  • Literature review of recent studies on the bacterial BAM complex.
  • Analysis of structural and functional data from various research groups.

Main Results:

  • Significant progress has been made in elucidating the structure of the BAM complex.
  • Key insights into the mechanism of β-barrel protein assembly have been gained.
  • The role of the BAM complex in bacterial outer membrane homeostasis is increasingly understood.

Conclusions:

  • The bacterial BAM complex is a dynamic machine essential for Gram-negative bacteria.
  • Further research into BAM complex structure and function holds potential for novel therapeutic strategies against bacterial infections.