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相关概念视频

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.4K
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...
7.4K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

11.0K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
11.0K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

8.1K
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.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
8.1K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.9K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.9K
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

1.0K
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...
1.0K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.6K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
19.6K

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相关实验视频

Updated: Apr 6, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

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

Published on: July 4, 2016

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聚处理和分泌载体的晶体结构

David Yin-wei Lin1, Shuo Huang2, Jue Chen1

  • 11] Laboratory of Membrane Biology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA [2] Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.

Nature
|July 24, 2015
PubMed
概括

含有酶的ATP结合盒载体 (PCAT) 是简单的细菌蛋白质分泌机器. 晶体结构揭示了ATP结合如何调节PCAT

科学领域:

  • 微生物学和分子生物学
  • 蛋白质分泌机制
  • 细菌细胞生物学

背景情况:

  • 细菌利用分泌的和蛋白质进行通信,竞争和宿主操纵.
  • 跨越细菌膜的蛋白质转移涉及不同的机器.
  • 含有酶的ATP结合盒传输体 (PCAT) 是这些系统的一个结构简单的类别.

研究的目的:

  • 阐明PCAT在蛋白质转位中的结构和功能机制.
  • 研究ATP结合在调节PCAT活动和基质加工中的作用.

主要方法:

  • 来自Clostridium热细胞的PCAT1的X射线晶体学
  • 生物化学测定以评估蛋白酶活性和转位通路功能.

主要成果:

  • 确定PCAT1的晶体结构,显示出一个大的α-螺旋转位路径.
  • 证明该通路可以容纳小的折叠蛋白质.
  • 显示ATP结合动态控制通路访问和蛋白酶活动,合基质加工到出口.

结论:

  • 在PCAT中使用依赖ATP的机制来协调基质的成熟和转移.
  • 阐明的机制为细菌蛋白质分泌和潜在的治疗点提供了洞察力.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

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