相关实验视频

Updated: Jun 7, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

对由 Pseudomonas aeruginosa 来源的阳性酸盐调节剂 MucP 调节的膜内蛋白质解的结构洞察

Xiaorui Lou¹, Shanshan Li¹, Yanan Wang¹

¹College of Life Sciences, State Key Laboratory of Medicinal Chemical Biology, Nankai International Advanced Research Institute (Shenzhen Futian), Nankai University, Tianjin 300071, China.

Biochemical and biophysical research communications

|November 20, 2024

概括

调节的内膜蛋白解涉及连续的蛋白酶裂变. 在Pseudomonas aeruginosa中,MucP (Site-2蛋白酶) 在 AlgW (Site-1蛋白酶) 之后分裂MucA,影响生物膜的形成.

科学领域:

微生物学微生物学
结构生物学结构生物学
生物化学生化学

背景情况:

调节性内膜蛋白解 (RIP) 是一种蛋白质加工的保存机制.
Pseudomonas aeruginosa 中的 MucABCD 系统调节抗西格玛因子 MucA,控制酸盐的产生.
MucA是由Site-1蛋白酶AlgW和Site-2蛋白酶MucP进行裂变的.

研究的目的:

阐明MucP在受调节的内膜蛋白解中的功能的结构基础.
了解MucP及其基质MucA之间的相互作用.

主要方法:

对MucP PDZ1和PDZ2域的高分辨率晶体结构的确定.
对MucP-MucA相互作用的结构和结合分析.
对 Pseudomonas aeruginosa 菌株具有 mucP 和 algW 突变的表型分析.

主要成果:

晶体结构显示MucP PDZ2与MucA的AlgW裂变后的C终端Ala136结合.
PDZ1域的结合槽被一个α螺旋阻塞.
MucP和AlgW对于Pseudomonas aeruginosa生物膜的形成至关重要.

结论:

MucP作为Site-2蛋白酶起作用,在Site-1分裂后识别MucA的C端.
对MucP-MucA相互作用的结构洞察力为了解RIP提供了基础.
MucP对于Pseudomonas aeruginosa的毒性,特别是生物膜的形成至关重要.

关键词:

酸生物合成这就是 MucPP.这是一个PDZ域名.伪omonas aeruginosa 这种类型的病毒.调节的内膜蛋白解.

更多相关视频

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

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

Published on: December 17, 2013

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

相关概念视频

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

The Proteasome Structure

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Archaeal Cell Wall

Archaeal Cell Wall

Archaeal cell walls are structurally and compositionally distinct from their bacterial counterparts, lacking the characteristic peptidoglycan layer found in most bacteria. Instead, archaeal cell walls exhibit remarkable diversity, utilizing materials such as pseudomurein, polysaccharides, and proteins to construct their protective outer layers. This structural flexibility is closely tied to archaea's ecological adaptability.S-Layers: The Common Archaeal Cell WallThe S-layer is the most...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Structure of Porins

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...