[{"quality_controlled":"1","author":[{"first_name":"Ziyu","full_name":"Zhao, Ziyu","id":"a63fe682-9f3a-11ee-bf8c-cfdf919b9850","last_name":"Zhao"},{"full_name":"Sazanov, Leonid A","first_name":"Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-0977-7989","last_name":"Sazanov"}],"doi":"10.1016/j.molcel.2026.05.026","_id":"22148","publication":"Molecular Cell","type":"journal_article","citation":{"ista":"Zhao Z, Sazanov LA. Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. Molecular Cell.","short":"Z. Zhao, L.A. Sazanov, Molecular Cell (n.d.).","chicago":"Zhao, Ziyu, and Leonid A Sazanov. “Structure of E. Coli Twin-Arginine Translocase (Tat) Complex with Bound Cargo.” <i>Molecular Cell</i>. Elsevier, n.d. <a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">https://doi.org/10.1016/j.molcel.2026.05.026</a>.","mla":"Zhao, Ziyu, and Leonid A. Sazanov. “Structure of E. Coli Twin-Arginine Translocase (Tat) Complex with Bound Cargo.” <i>Molecular Cell</i>, Elsevier, doi:<a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">10.1016/j.molcel.2026.05.026</a>.","ieee":"Z. Zhao and L. A. Sazanov, “Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo,” <i>Molecular Cell</i>. Elsevier.","ama":"Zhao Z, Sazanov LA. Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. <i>Molecular Cell</i>. doi:<a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">10.1016/j.molcel.2026.05.026</a>","apa":"Zhao, Z., &#38; Sazanov, L. A. (n.d.). Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">https://doi.org/10.1016/j.molcel.2026.05.026</a>"},"acknowledgement":"We thank IST Austria for providing the funding. We thank IST Austria EM facility for the use of Titan Krios TEM. Data processing was performed using IST high-performance computer cluster. We thank Dr. R. Roemhild and Professor C. Guet (ISTA) for help in constructing Tat deletion strains and Dr. A. Charnagalov (ISTA) for technical help.","ddc":["570"],"external_id":{"biorxivid":["10.1101/2025.09.16.676506"]},"title":"Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo","language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1016/j.molcel.2026.05.026","open_access":"1"}],"related_material":{"record":[{"id":"22189","relation":"research_data","status":"for_moderation"}]},"abstract":[{"lang":"eng","text":"How the twin-arginine translocase (Tat) system transports fully folded substrate proteins across cellular membranes without disrupting membrane integrity has been a fundamental question in cell biology for decades. The Tat system, found in prokaryotes and plant organelles, recognizes a cargo signal peptide via a conserved twin-arginine motif. The multi-subunit Tat complex facilitates the proton-motive-force-dependent translocation process, yet its overall architecture has remained unknown. Here, we present the cryo-electron microscopy (cryo-EM) structure of the Escherichia coli (E. coli) trimeric TatB₃C₃ complex with bound substrate SufI, assembled in vivo. The complex adopts an unusual, wide-open, bowl-shaped architecture with a polar inner cavity. Unexpectedly, the cargo is engaged in a dual-contact mode: while the signal peptide binds inside one TatBC unit, the folded domain docks tightly onto an adjacent unit, possibly performing a proofreading function. This structure provides a mechanistic framework for substrate engagement and suggests the direct involvement of the entire Tat complex in substrate translocation."}],"day":"22","date_created":"2026-06-28T22:01:35Z","scopus_import":"1","year":"2026","status":"public","researchdata_availability":"yes","corr_author":"1","biorxivid":1,"has_accepted_license":"1","OA_place":"publisher","publication_identifier":{"issn":["1097-2765"],"eissn":["1097-4164"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","tmp":{"short":"CC BY-NC (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)"},"OA_type":"hybrid","oa":1,"article_processing_charge":"Yes (via OA deal)","department":[{"_id":"LeSa"}],"month":"06","date_published":"2026-06-22T00:00:00Z","article_type":"original","publication_status":"inpress","date_updated":"2026-06-29T12:55:19Z","supplementarymaterial":"yes","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"ScienComp"}],"publisher":"Elsevier","dataavailabilitystatement":"This study did not generate new unique reagents. Strains and plasmids generated in this study are available from the lead contact without restrictions.\r\n• Source data are provided within this paper. The cryo-EM map is deposited in the Electron Microscopy Data Bank under accession number EMD-53848. The model is deposited in the Protein Data Bank under accession number 9R91. The structural data are publicly available as of the date of publication. Raw images of spot assays, SDS-PAGE and BN-PAGE gels with Coomassie staining and immunoblot images are available at Mendeley Data (https://doi.org/10.17632/v2g3p9n985.1).\r\n• This paper does not report original code.\r\n• Any additional information required to reanalyze the data reported in this paper is available from the lead contact upon request.","das_tickbox":"1"}]