| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yidC |
| Uniprot No | A8A6G7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-548aa |
| 氨基酸序列 | MDSQRNLLVIALLFVSFMIWQAWEQDKNPQPQAQQTTQTTTTAAGSAADQGVPASGQGKLISVKTDVLDLTINTRGGDVEQALLPAYPKELNSTQPFQLLETSPQFIYQAQSGLTGRDGPDNPANGPRPLYNVEKDAYVLAEGQNELQVPMTYTDAAGNTFTKTFVLKRGDYAVNVNYNVQNAGEKPLEISTFGQLKQSITLPPHLDTGSSNFALHTFRGAAYSTPDEKYEKYKFDTIADNENLNISSKGGWVAMLQQYFATAWIPHNDGTNNFYTANLGNGIAAIGYKSQPVLVQPGQTGAMNSTLWVGPEIQDKMAAVAPHLDLTVDYGWLWFISQPLFKLLKWIHSFVGNWGFSIIIITFIVRGIMYPLTKAQYTSMAKMRMLQPKIQAMRERLGDDKQRISQEMMALYKAEKVNPLGGCFPLLIQMPIFLALYYMLMGSVELRQAPFALWIHDLSAQDPYYILPILMGVTMFFIQKMSPTTVTDPMQQKIMTFMPVIFTVFFLWFPSGLVLYYIVSNLVTIIQQQLIYRGLEKRGLHSREKKKS |
| 预测分子量 | 63.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于YidC重组蛋白的3篇代表性文献概览：
1. **《Structural insight into the role of the YidC protein in membrane protein assembly》**
- 作者：Kumazaki, K. et al.
- 摘要：通过X射线晶体学解析了来自嗜热菌的YidC重组蛋白的晶体结构(分辨率2.4 Å)，揭示了其跨膜螺旋的排列特征及带正电荷的亲水面，为YidC通过静电作用介导膜蛋白插入的机制提供了结构基础。
2. **《YidC mediates membrane protein insertion in bacteria》**
- 作者：Sachelaru, I. et al.
- 摘要：利用体外重构实验证明，重组YidC蛋白独立于Sec转位酶系统，可直接协助特定膜蛋白(如噬菌体M13外壳蛋白)插入细菌内膜，并阐明了其底物选择性与跨膜结构域相互作用的分子机制。
3. **《Reconstitution of the YidC-dependent insertion of Pf3 coat protein into proteoliposomes》**
- 作者：van der Laan, M. et al.
- 摘要：通过将纯化的重组YidC整合到脂质体中，成功重建了噬菌体Pf3外壳蛋白的跨膜插入过程，证明YidC单独具有催化膜蛋白折叠的活性，并揭示了脂质组成对其功能的影响。
注：以上文献均聚焦YidC重组蛋白的生化功能验证及结构机制研究，涵盖领域经典及近年进展。如需扩展，可补充YidC与伴侣蛋白协同作用的相关研究(如2020年《Nature》期刊中Collinson团队发表的冷冻电镜研究)。
YidC is a highly conserved membrane protein integral to bacterial inner membranes, playing a pivotal role in the insertion, folding, and assembly of membrane proteins. Identified initially in *Escherichia coli*, YidC belongs to the *insertase* family, functioning either independently or in concert with the Sec translocon to facilitate the biogenesis of α-helical membrane proteins. Its homologs, such as Oxa1 in mitochondrial inner membranes and Alb3 in chloroplasts, underscore its evolutionary significance in membrane protein biogenesis across prokaryotic and eukaryotic systems.
YidC operates through a unique mechanism. Unlike the Sec system, which primarily handles unfolded polypeptide chains, YidC interacts with nascent membrane proteins during or after their translocation, aiding in their lateral integration into the lipid bilayer. Structural studies reveal that YidC possesses six transmembrane helices, with a large hydrophilic domain protruding into the cytoplasm. This charged region likely mediates substrate recognition and chaperoning, while its transmembrane groove stabilizes hydrophobic segments of client proteins. Notably, YidC is essential for the assembly of energy-transducing complexes (e.g., ATP synthase) and virulence factors in pathogenic bacteria, linking its function to cellular energetics and microbial pathogenicity.
Research on YidC has expanded due to its potential as a therapeutic target. Inhibitors disrupting YidC could combat antibiotic-resistant pathogens by impairing membrane protein biogenesis. Additionally, YidC serves as a model system to study membrane protein insertion mechanisms, offering insights into diseases linked to defective protein folding, such as neurodegenerative disorders. Despite progress, key questions remain about its substrate specificity, interplay with other translocases, and structural dynamics during membrane protein assembly. Advances in cryo-EM and single-molecule techniques continue to unravel these mysteries, solidifying YidC's role as a cornerstone in membrane biology.
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