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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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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.
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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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.
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Structure of Porins01:21

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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...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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The Name Is Barrel, β-Barrel.

Scout Hayashi1, Susan K Buchanan1, Istvan Botos2

  • 1Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 13, 2024
PubMed
Summary
This summary is machine-generated.

Beta-barrel outer membrane proteins (OMPs) are crucial in Gram-negative bacteria, mitochondria, and chloroplasts. This review covers their functions, folding mechanisms, and future research directions.

Keywords:
BAM complexOuter membrane β-barrelsSAM complexTonB-dependent transporter

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Beta-barrels are integral membrane proteins forming a cylindrical, anti-parallel beta-sheet structure.
  • These proteins feature a hydrophobic exterior and a hydrophilic interior, facilitating membrane integration.
  • Beta-barrel outer membrane proteins (OMPs) are abundant in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts.

Purpose of the Study:

  • To review the diverse functional classes of beta-barrel OMPs.
  • To discuss the mechanisms of beta-barrel OMP folding into cellular membranes.
  • To explore the future prospects and applications of beta-barrel OMP research.

Main Methods:

  • Literature review of existing research on beta-barrel OMPs.
  • Analysis of structural and functional data.
  • Discussion of current and emerging research trends.

Main Results:

  • Beta-barrel OMPs exhibit a wide range of functions, including nutrient transport, secretion, and virulence.
  • Specific pathways and molecular chaperones are involved in the correct folding of OMPs.
  • Ongoing research is uncovering novel applications for these proteins.

Conclusions:

  • Beta-barrel OMPs are essential components of cellular membranes with diverse biological roles.
  • Understanding OMP folding is critical for comprehending their function and for biotechnological applications.
  • Future research holds promise for advancing our knowledge and utilization of beta-barrel OMPs.