Structure最新文献_第8页

Structural insights into ZBTB20 action at the AFP promoter ZBTB20在AFP启动子上作用的结构见解

IF 5.7 2区生物学

Structure Pub Date : 2025-06-09 DOI: 10.1016/j.str.2025.05.009

Lingna Yang, Huajiao Xie, Xiaoqing Wan, Mengfeng Li, Mengqi Lv, Yi Duan, Yunyu Shi, Weiping J. Zhang, Fudong Li

引用次数: 0

Secondary chelation through shared water provides ion selectivity in bacterial sodium channels 通过共享水的二级螯合作用在细菌钠离子通道中提供离子选择性

IF 5.7 2区生物学

Structure Pub Date : 2025-06-09 DOI: 10.1016/j.str.2025.05.010

Yury A. Trofimov, Anton O. Chugunov, Alexander A. Vassilevski

{"title":"Secondary chelation through shared water provides ion selectivity in bacterial sodium channels","authors":"Yury A. Trofimov, Anton O. Chugunov, Alexander A. Vassilevski","doi":"10.1016/j.str.2025.05.010","DOIUrl":"https://doi.org/10.1016/j.str.2025.05.010","url":null,"abstract":"Selective ion conductance through sodium channels has been intensely investigated for decades. Here, we focus on the sodium and potassium hydration shell structure and propose the mechanism of Na+ over K+ selectivity in the bacterial sodium channel NavMs. We suggest that the channel selectivity filter forms hydrogen bonds with Na+ hydration shell in a perfect octahedral stereometry, which mimics bulk water and provides high Na+ conductance. Using molecular dynamics simulations, we reveal a conserved ion-binding site formed by carboxyl/carbonyl groups, where both Na+ and K+ remain fully hydrated. While passing through the selectivity filter, Na+ octahedral shell remains unhindered, while K+ square antiprismatic shell is squeezed, creating an energy barrier for K+ current. In contrast to K+-channels, where the selectivity filter interacts with the permeating ions directly (“primary” chelation), NavMs gropes the ion hydration shell, performing “secondary” chelation. This ion recognition mechanism is probably widespread in other channels and pores.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"7 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144237991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural plasticity of bacterial ubiquitin-like proteins in stress sensing 细菌泛素样蛋白在应激感知中的结构可塑性

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.05.002

Weixun Li, Xiang Gao

引用次数: 0

Color mapping of multitarget protein clusters 多靶点蛋白簇的颜色映射

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.05.004

Hirushi Gunasekara, Ying S. Hu

引用次数: 0

Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome 抗疟药物青蒿素稳定PfRACK1与核糖体的结合

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.05.008

Ka Diam Go, Xin-Fu Yan, Grennady Wirjanata, Rya Ero, Samuel Pazicky, Jerzy Dziekan, Seth Tjia, Julien Lescar, Zbynek Bozdech, Yong-Gui Gao

引用次数: 0

Need for speed: Mass photometry as a sample analysis tool for structural studies 需要速度：质谱法作为结构研究的样品分析工具

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.04.014

Lauren E. Vostal

引用次数: 0

Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment 淀粉样蛋白形成片段对人类CPEB3朊病毒功能调控的结构见解

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.05.007

Maria D. Flores, Michael R. Sawaya, David R. Boyer, Samantha Zink, Susanna Tovmasyan, Adrian Saucedo, Logan S. Richards, Chih-Te Zee, Jorge Cardenas, Luana Fioriti, Jose A. Rodriguez

{"title":"Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment","authors":"Maria D. Flores, Michael R. Sawaya, David R. Boyer, Samantha Zink, Susanna Tovmasyan, Adrian Saucedo, Logan S. Richards, Chih-Te Zee, Jorge Cardenas, Luana Fioriti, Jose A. Rodriguez","doi":"10.1016/j.str.2025.05.007","DOIUrl":"https://doi.org/10.1016/j.str.2025.05.007","url":null,"abstract":"The cytoplasmic polyadenylation-element-binding-protein-3 (CPEB3) is a functional prion thought to modulate protein synthesis and enable consolidation of long-term memory in neurons. We report a cryoelectron microscopy (cryo-EM) structure of amyloid fibrils grown in vitro from the first prion-like domain of human CPEB3 (hCPEB3), revealing their ordered 49-residue core, spanning L103 to F151. CPEB3 lacking that segment coalesces into abnormal puncta in cells compared to wild-type CPEB3, localizes away from dormant p-bodies and toward stress granules, and lacks the ability to influence protein synthesis in neurons. Fluorescence-guided cryo-focused ion beam (cryo-FIB) milling and cryo-electron tomography (cryo-ET) applied to neuronal cells expressing CPEB3 reveal CPEB3-GFP signal from lamellae enriched in multivesicular bodies (MVBs), cavernous multilamellar compartments, and bundled filaments, suggesting a state of induced cellular stress. Accordingly, cells expressing wild-type CPEB3 are less viable than those expressing CPEB3 without its amyloid core, suggesting human CPEB3 regulation may be required to overcome the liability associated with its self-assembly in cells.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"42 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-06-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144219116","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The effect of G-quadruplexes on TDP43 condensation, distribution, and toxicity g -四聚物对TDP43缩聚、分布及毒性的影响

IF 5.7 2区生物学

Structure Pub Date : 2025-06-05 DOI: 10.1016/j.str.2025.05.006

Emily G. Oldani, Kevin M. Reynolds Caicedo, McKenna E. Spaeth Herda, Adam H. Sachs, Erich G. Chapman, Sunil Kumar, Daniel A. Linseman, Scott Horowitz

{"title":"The effect of G-quadruplexes on TDP43 condensation, distribution, and toxicity","authors":"Emily G. Oldani, Kevin M. Reynolds Caicedo, McKenna E. Spaeth Herda, Adam H. Sachs, Erich G. Chapman, Sunil Kumar, Daniel A. Linseman, Scott Horowitz","doi":"10.1016/j.str.2025.05.006","DOIUrl":"https://doi.org/10.1016/j.str.2025.05.006","url":null,"abstract":"Many proteins implicated in neurodegenerative diseases (e.g., trans-active response DNA binding protein 43 kDa [TDP43]) interact with nucleic acids, including RNA G-quadruplexes (G4s). We here investigate whether RNA G4s play a role in TDP43 condensation in biophysical and cellular models. We find that G4s modulate TDP43 aggregation in vitro and condensation in multiple cell types, including yeast, HEK293T, and motor-neuron-like NSC-34 cells. In yeast cells, treatment with G4s causes increased TDP43 accumulation in cells before cellular death. In HEK293T cells expressing TDP43, incubation with G4-binding small molecules causes an increase in G4 stability that also stabilizes TDP43 and reduces TDP43 condensation induced by proteasomal or oxidative stress. Finally, in NSC-34 cells overexpressing exogenous TDP43, we show that G4s co-localize with TDP43 condensates under stress conditions, and treatment with G4-binding small molecules decreases TDP43-mediated toxicity. Together, these findings suggest exploring treating protein misfolding diseases by targeting specific RNA structures such as G4s.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"36 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-06-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144219118","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Biochemical analysis of PD-L1 ubiquitination by CRL3SPOP, ARIH1, and NEDD4 family ubiquitin ligases CRL3SPOP、ARIH1和NEDD4家族泛素连接酶对PD-L1泛素化的生化分析

IF 5.7 2区生物学

Structure Pub Date : 2025-06-04 DOI: 10.1016/j.str.2025.05.005

Guojiao Xie, Lin Gao, Renee Lu, Linxia Tian, Tiantian Zheng, Xinning Li, Yongjun Dang, Philip A. Cole, Xian Yu, Hanjie Jiang, Zan Chen

{"title":"Biochemical analysis of PD-L1 ubiquitination by CRL3SPOP, ARIH1, and NEDD4 family ubiquitin ligases","authors":"Guojiao Xie, Lin Gao, Renee Lu, Linxia Tian, Tiantian Zheng, Xinning Li, Yongjun Dang, Philip A. Cole, Xian Yu, Hanjie Jiang, Zan Chen","doi":"10.1016/j.str.2025.05.005","DOIUrl":"https://doi.org/10.1016/j.str.2025.05.005","url":null,"abstract":"As a key immune checkpoint ligand, PD-L1 is a critical target in cancer immunotherapy. While multiple E3 ubiquitin ligases including CRL3SPOP, ARIH1, and NEDD4 have been implicated in PD-L1 degradation, the precise enzymatic mechanisms remain unclear. In this study, we systematically compared the enzymatic activities of CRL3SPOP, ARIH1, and NEDD4 ligases toward the cytoplasmic domain of PD-L1 through in vitro reconstitution with purified components. ARIH1, rather than CRL3SPOP, independently ubiquitinates PD-L1. We reveal a mechanism where ARIH1 acts as a substrate receptor and cooperates with CRLs to catalyze PD-L1 ubiquitination. We also biochemically validated the E3 ligase activity of the NEDD4 family E3s toward PD-L1. By using liposomes in the enzymatic assays, we show that phosphorylation enhances PD-L1 ubiquitination through disrupting its membrane association. Our study provides further biochemical insights into PD-L1 ubiquitination, which advances our understanding of the molecular details of PD-L1 regulation.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"8 1","pages":""},"PeriodicalIF":5.7,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144211518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural insights into the interaction of Hir2 and Hpc2 in the yeast Hir histone chaperone complex 酵母Hir组蛋白伴侣复合物中Hir2和Hpc2相互作用的结构见解

IF 5.7 2区生物学

Structure Pub Date : 2025-05-30 DOI: 10.1016/j.str.2025.05.003

Chu-Hsin Tseng, Wen-Lin Hsieh, Wesley Tien Chiang, Nien-Jen Hu, Chia-Liang Lin

引用次数: 0