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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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...

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Related Experiment Video

Updated: Jun 4, 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

β-Barrel membrane protein assembly by the Bam complex.

Christine L Hagan1, Thomas J Silhavy, Daniel Kahne

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. clhagan@fas.harvard.edu

Annual Review of Biochemistry
|March 5, 2011
PubMed
Summary

Beta-barrel membrane proteins are crucial for cellular functions. Recent studies are revealing the mechanisms of their assembly, offering insights into membrane protein biogenesis.

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Last Updated: Jun 4, 2026

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
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Published on: July 4, 2016

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Published on: December 17, 2013

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Beta-barrel proteins are essential membrane components in bacteria, mitochondria, and chloroplasts.
  • These proteins require specific handling and assembly pathways distinct from alpha-helical proteins.
  • A conserved assembly component exists across species, from bacteria to humans.

Purpose of the Study:

  • To elucidate the mechanism of beta-barrel protein assembly in membranes.
  • To understand how assembly complexes bind, fold, and insert beta-barrel proteins.
  • To compare beta-barrel assembly with alpha-helical membrane protein assembly.

Main Methods:

  • Structural studies
  • Biochemical assays
  • Genetic analyses

Main Results:

  • Recent studies have identified key components and elucidated elements of the beta-barrel assembly pathway.
  • The assembly complex facilitates the binding, folding, and insertion of beta-barrel proteins.
  • Differences in handling beta-barrel vs. alpha-helical proteins are crucial for efficient transport.

Conclusions:

  • The mechanism of beta-barrel assembly is becoming clearer through integrated studies.
  • Comparing beta-barrel and alpha-helical assembly may reveal general principles of membrane protein biogenesis.
  • Understanding these pathways is vital for comprehending cellular membrane functions.