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関連する概念動画

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.2K
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...
5.2K
Structure of Porins01:21

Structure of Porins

4.1K
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...
4.1K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
5.1K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.3K
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...
7.3K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.7K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.7K
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

980
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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関連する実験動画

Updated: Mar 25, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

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BAM複合体による外膜タンパク質挿入の構造的基礎

Yinghong Gu1, Huanyu Li1, Haohao Dong1

  • 1Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.

Nature
|February 23, 2016
PubMed
まとめ

バクテリアの外膜タンパク質組成機構 (BAM) のメカニズムは今より明確になっています. 構造の研究では,BamaAと関連するタンパク質が,新しい外膜タンパク質 (OMP) を細胞包膜に挿入するためにどのように回転するかを明らかにしています.

さらに関連する動画

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

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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

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関連する実験動画

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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
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科学分野:

  • 構造生物学
  • 分子生物学
  • 生物化学

背景:

  • 外膜タンパク質 (OMP) は,グラム陰性細菌,ミトコンドリア,クロロプラストにとって極めて重要です.
  • βバレル組立装置 (BAM) 複合体は,OMPを外膜に挿入し折りたたむことを容易にする.
  • 構造的なデータが不足しているため,BAM媒介のOMP生殖の正確なメカニズムはほとんど不明である.

研究 の 目的:

  • BAM複合体による外膜タンパク質挿入のメカニズムを解明する.
  • エシェリキア・コライのBAM複合体に関する高解像度構造の洞察を提供すること.
  • OMP 生成過程におけるBAMサブユニット間のダイナミックな相互作用を理解する.

主な方法:

  • 異なる状態のBAM複合体の構造を決定するX線結晶学.
  • BAM複合体の構成要素の機能を研究する生化学的分析
  • BAM複合体内のダイナミックな動きを分析するための分子ダイナミクスシミュレーション.

主要な成果:

  • Escherichia coli BAM複合体の2つの異なる結晶構造が決定されました:内側開いた状態と横側開いた状態です.
  • 構造は,4つのリポタンパク質 (BamB-BamE) と関連したBamAの5つのポリペプチド輸送関連ドメインによって形成されたリング構造を明らかにする.
  • 構造的および機能的データは,Bammaのβバレルに対する関連リポタンパク質の回転が新生OMPの挿入を誘導することを示しています.

結論:

  • この研究は,BAM複合体の前例のない構造のスナップショットを提供し,そのダイナミックな性質を明らかにします.
  • この発見は,BAM複合体が介在するOMP挿入のための回転ベースのメカニズムを明らかにしています.
  • この研究は 重要な膜タンパク質の 生成における 根本的な過程の理解を 大きく前進させています