StructurePub Date : 2026-05-07Epub Date: 2026-03-16DOI: 10.1016/j.str.2026.02.010
Amit Kumar, Kuei-Chen Wang, Partho Ghosh
{"title":"Structural mechanisms for the recruitment of factor H by Streptococcus pyogenes.","authors":"Amit Kumar, Kuei-Chen Wang, Partho Ghosh","doi":"10.1016/j.str.2026.02.010","DOIUrl":"10.1016/j.str.2026.02.010","url":null,"abstract":"<p><p>The bacterial pathogen Streptococcus pyogenes (Strep A) recruits the complement regulator factor H (FH) to its surface using M proteins and FbaA. However, no conserved FH-binding sequence pattern is evident in these proteins. To address this, we determined the structures of M5 protein, M6 protein, and FbaA fragments complexed with FH domains 6 and 7. M5 and M6 proteins formed dimeric α-helical coiled coils, as expected, while FbaA formed a monomeric three-helix bundle preceded by a loop. Each Strep A protein had a different FH-binding mode, and distinct FH-binding sequence patterns were constructed for each based on substitution mutagenesis. About half of the known 250 Strep A strains were identified to have FH-binding patterns, with the majority due to FbaA as compared to M or M-like Enn proteins. Our structural and functional elucidation of the mechanism of FH recruitment is applicable to the precise investigation of its role in Strep A virulence.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":" ","pages":"778-789.e4"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13002132/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147475254","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.04.002
Ming-Daw Tsai, Matthias Wolf, Chiung-Wen Mary Chang, Wah Chiu
{"title":"Cryo-EM in enzymology and dynamics.","authors":"Ming-Daw Tsai, Matthias Wolf, Chiung-Wen Mary Chang, Wah Chiu","doi":"10.1016/j.str.2026.04.002","DOIUrl":"https://doi.org/10.1016/j.str.2026.04.002","url":null,"abstract":"<p><p>Pacifichem 2025 is a joint chemical congress of chemical societies from Pacific basin regions, held in Hawaii every 5 years since 1984. It covers all disciplines of chemistry. The meeting in December 15-20, 2025, included for the first time a cryo-electron microscopy symposium with 36 speakers and a poster session.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"675-680"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147856934","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.04.007
Mikhail Kudryashev, Clorice R Reinhardt, Alec H Follmer, Michael C Thompson
{"title":"Introducing Mikhail Kudryashev, Clorice R. Reinhardt, Alec H. Follmer, and Michael C. Thompson.","authors":"Mikhail Kudryashev, Clorice R Reinhardt, Alec H Follmer, Michael C Thompson","doi":"10.1016/j.str.2026.04.007","DOIUrl":"https://doi.org/10.1016/j.str.2026.04.007","url":null,"abstract":"<p><p>This voices article features four impressive group leaders who participated in the recent \"9th Ringberg Workshop on Structural Biology with XFELs\", organized by Ilme Schlichting from the Max Planck Institute for Medical Research in Heidelberg. We asked them to tell us more about their career paths, research interests, and what inspires their work.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"681-684"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147857006","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.03.007
Kishore K Mahalingan
{"title":"A liquid engine: How Spef1 droplets set the ciliary beat.","authors":"Kishore K Mahalingan","doi":"10.1016/j.str.2026.03.007","DOIUrl":"https://doi.org/10.1016/j.str.2026.03.007","url":null,"abstract":"<p><p>In this issue of Structure, Ren et al.<sup>1</sup> show that the microtubule-associated protein Spef1 undergoes liquid-liquid phase separation mediated by its uniquely charged coiled-coil domain. These dynamic Spef1 condensates enrich tubulin to drive central-pair microtubule (CP-MT) assembly, providing a long-sought mechanistic explanation for CP-MT assembly and planar ciliary beating.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"685-686"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147856797","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.04.004
Luke M Tomasovic, Sofia Farhangnia, Jamie B Spangler
{"title":"REAPing the benefits of comprehensive specificity profiling for therapeutic antibody development.","authors":"Luke M Tomasovic, Sofia Farhangnia, Jamie B Spangler","doi":"10.1016/j.str.2026.04.004","DOIUrl":"https://doi.org/10.1016/j.str.2026.04.004","url":null,"abstract":"<p><p>In this issue of Structure, Dai et al.<sup>1</sup> systematically profile off-target reactivity across 174 clinical-stage and approved antibody therapeutics, revealing that 28% bind unintended human extracellular proteins. They validate functionally relevant off-target interactions and show that antibody engineering can eliminate these liabilities while maintaining target affinity and favorable developability properties.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"687-689"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147857097","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.04.008
Spencer J Rothfuss, Qiangjun Zhou
{"title":"Let there be light: Targeted fluorescent labels illuminate cryo-FIB/ET of synapses.","authors":"Spencer J Rothfuss, Qiangjun Zhou","doi":"10.1016/j.str.2026.04.008","DOIUrl":"https://doi.org/10.1016/j.str.2026.04.008","url":null,"abstract":"<p><p>Focused ion beam milling exposes buried cellular regions, such as chemical synapses within neuronal networks, for high-resolution electron microscopy. In this issue of Structure, Do et al.<sup>1</sup> use fluorescent tags to target milling and imaging to synapses, successfully removing confounding material and capturing synaptic ultrastructure in high resolution.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"692-693"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147857012","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}
StructurePub Date : 2026-05-07Epub Date: 2026-03-03DOI: 10.1016/j.str.2026.02.004
Haonan D Xu, Mihaly Badonyi, Marilyn Paul, Watanyoo Sopipong, Stuart A MacGowan, Joseph A Marsh, David H Murray
{"title":"Structural extension of the human exocyst is enabled by a minimal interface.","authors":"Haonan D Xu, Mihaly Badonyi, Marilyn Paul, Watanyoo Sopipong, Stuart A MacGowan, Joseph A Marsh, David H Murray","doi":"10.1016/j.str.2026.02.004","DOIUrl":"10.1016/j.str.2026.02.004","url":null,"abstract":"<p><p>In multicellular organisms, the machinery responsible for polarized trafficking directs constitutive cargo secretion at distinct sites of the plasma membrane, cilia, and junctional structures. Central to this machinery is the exocyst complex, which tethers cargo vesicles to their destination membrane, alongside other intracellular membrane tethering roles. Precisely how the exocyst spatially integrates membranes and membrane resident binding partners is unclear. Here, we address the structural morphology and formation of the human exocyst complex. Through structural approaches coupled to predictive models, we determined that the exocyst and its subcomplexes have extended \"arm-like\" structures that help maximize its reach. Moreover, we demonstrate minimal intersubunit interaction, in contrast to prior models. Nucleation of the holocomplex occurs through a single site, explaining its spatial extension. Our results provide the biochemical basis for exocyst complex assembly, suggesting an ornate extended architecture.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":" ","pages":"870-879.e5"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147356150","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.04.009
Weiwei Wang
{"title":"Breaking symmetry: Homomeric glycine receptor joins the asymmetric gating club.","authors":"Weiwei Wang","doi":"10.1016/j.str.2026.04.009","DOIUrl":"https://doi.org/10.1016/j.str.2026.04.009","url":null,"abstract":"<p><p>In this issue of Structure, Klemm et al.<sup>1</sup> use well-designed biochemical conditions and show that a homomeric human glycine receptor opens in an asymmetric manner despite composed solely of the α2 subunits. This demonstrates an asymmetric gating mechanism more like heteromeric glycine receptors. Details of picrotoxin inhibition were further characterized.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"690-691"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147856961","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}
StructurePub Date : 2026-05-07DOI: 10.1016/j.str.2026.03.008
Ka Young Chung, Jun Xu
{"title":"Meet the authors: Ka Young Chung and Jun Xu.","authors":"Ka Young Chung, Jun Xu","doi":"10.1016/j.str.2026.03.008","DOIUrl":"https://doi.org/10.1016/j.str.2026.03.008","url":null,"abstract":"<p><p>In this meet-the-authors Q&A, we speak to Ka Young Chung from Sungkyunkwan University, Republic of Korea, and Jun Xu from the Southern University of Science and Technology, China, about their recent Structure paper entitled \"Ligand-specific conformational dynamics of the α2A-adrenergic receptor revealed by hydrogen-deuterium exchange mass spectrometry\" and their research and careers.</p>","PeriodicalId":22168,"journal":{"name":"Structure","volume":"34 5","pages":"694-695"},"PeriodicalIF":4.3,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147857077","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}