脂结银河体出口的结构基础由真菌细菌的ABC载体Wzm-Wztzt出口
Alisa A Garaeva1, Viktória Fabianová2, Karin Savková2
1Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland. alisa.garaeva@uzh.ch.
Nature communications
|March 17, 2026
概括
结核菌菌的细胞壁生物合成涉及由Wzm-Wzt ABC转运器运输的阿拉比诺. 低温EM结构揭示了细胞质门螺旋对于转移脂质结合的银河系前体至关重要.
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 生物化学
背景情况:
- 菌根菌具有独特的细胞外,含有阿拉比诺,对于细胞壁完整性至关重要.
- 阿拉比诺银河生物合成是结核病药物开发的目标.
- Wzm-Wzt ABC 输送器促进了阿拉比诺 galaktan 前体,脂结 galaktan (LLG) 的转移.
研究的目的:
- 为了阐明LLG通过Wzm-Wzt传送器转移的分子机制.
- 使用冷电子显微镜 (cryo-EM) 确定Wzm-Wzt函数的结构基础.
- 为了确定参与多糖体运输途径的关键残留物.
主要方法:
- 低温电子显微镜 (cryo-EM) 用于捕捉Wzm-Wzt的不同形状.
- 正义功能测试用于研究LLG转位通路中的保存残留物.
- 在运输过程中ATP水解的生物化学分析.
主要成果:
- Mycobacterium abscessus Wzm-Wzt的多个冷-EM结构显示出不同的运输周期构造.
- 细胞门螺旋 (GH) 被确定为聚糖类运输的关键.
- 证据表明顺序转移,疏水部分在多糖链之前.
- Wzm-Wzt通过开辟由ATP水解提供动力的连续通道来促进多糖体的运输.
结论:
- 这项研究提供了对阿拉伯银河系前体运输机制的原子层次见解.
- 细胞门螺旋是Wzm-Wzt传送器中一个关键的调节元件.
- 这些发现为设计针对菌根细胞壁生物合成的新药提供了基础.
更多相关视频
05:28Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
2.8K
06:47Author Spotlight: A Bicelle Crystallization Setup for ABC Transporter Membrane Proteins to Advance Drug Development
Published on: August 25, 2023
1.9K
相关概念视频
01:27ABC Transporters: Importer
3.7K
ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
3.7K
01:31ABC Transporters: Exporter
7.0K
ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
7.0K
01:19Formation of Lipopolysaccharides
892
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
892
01:26Bacterial Translocation and Protein Secretion
952
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...
952
01:32Export of Misfolded Proteins out of the ER
5.4K
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...
5.4K
01:24Oligosaccharide Assembly
3.8K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
3.8K