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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,9,15]]},"abstract":"<jats:p>\n                    Glycosylphosphatidylinositol (GPI) anchoring shapes eukaryotic cell-surface architecture and represents an attractive pathway for antifungal intervention. The first committed mannosylation step in GPI biosynthesis is catalyzed by GPI mannosyltransferase I (GPI-MT-I), a membrane-embedded enzyme complex essential for fungal cell-wall integrity and virulence. Despite its therapeutic potential, the molecular basis and chemical mechanism of this lipid-dependent glycosyltransferase have remained unclear. Here, we combine cryoelectron microscopy, chemical synthesis, and functional analyses to define the architecture, substrate recognition, and catalytic mechanism of fungal GPI-MT-I, the Gpi14-Pbn1 heterodimer. We captured catalytically distinct states of fungal GPI-MT-I, including a ternary complex simultaneously bound to dolichol-phosphate-mannose and GlcN-(acyl)phosphatidylinositol. These reveal a membrane-embedded reaction chamber containing a continuous substrate-binding tunnel, in which two amphipathic lipid substrates are positioned in a head-to-head configuration for glycosyl transfer. Structural and mutational analyses establish GPI-MT-I as a GT-C-fold inverting glycosyltransferase and support a concerted S\n                    <jats:sub>N<\/jats:sub>\n                    2-like mechanism centered on the conserved catalytic aspartate Asp38. Comparative analyses reveal pronounced fungal-specific structural features with therapeutic potential, explaining the functional incompatibility across species. These findings provide a molecular and chemical blueprint for lipid-linked glycosyl transfer in membranes and a foundation for structure-guided antifungal drug development.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2617140123","type":"journal-article","created":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T17:02:15Z","timestamp":1789059735000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Structural and mechanistic insights into the fungal glycosylphosphatidylinositol mannosyltransferase I complex"],"prefix":"10.1073","volume":"123","author":[{"given":"Jia","family":"Liu","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00p991c53","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Huazhong University of Science 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Gupta, S. Brunak, \u201cPrediction of glycosylation across the human proteome and the correlation to protein function\u201d in Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing (2022), pp. 310\u2013322.","journal-title":"Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing"},{"key":"e_1_3_4_31_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkq366"},{"key":"e_1_3_4_32_2","article-title":"Molecular insights into fungal glycosylphosphatidylinositol transamidase complex","volume":"13","author":"Hua Z.","year":"2026","unstructured":"Z. Hua , Molecular insights into fungal glycosylphosphatidylinositol transamidase complex. Adv. Sci. (Weinheim, Baden-Wurttemberg, Germany) 13, e11340 (2026).","journal-title":"Adv. Sci. 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Sun , Structural insights into the Glycosylphosphatidylinositol Mannosyltransferase I complex from Candida glabrata. J. Fungi (Basel, Switzerland) 11, 819 (2025).","journal-title":"J. Fungi (Basel, Switzerland)"},{"key":"e_1_3_4_51_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-41747-z"},{"key":"e_1_3_4_52_2","doi-asserted-by":"publisher","DOI":"10.1021\/acschembio.1c00465"},{"key":"e_1_3_4_53_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja1009037"},{"key":"e_1_3_4_54_2","doi-asserted-by":"publisher","DOI":"10.1021\/acs.orglett.5c02580"},{"key":"e_1_3_4_55_2","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.4169"},{"key":"e_1_3_4_56_2","doi-asserted-by":"publisher","DOI":"10.1002\/yea.1397"},{"key":"e_1_3_4_57_2","unstructured":"J. Liu The cryo-EM map of GPI-MT-I complex. EMDB. https:\/\/www.ebi.ac.uk\/emdb\/EMD-68960. Deposited 6 February 2026."},{"key":"e_1_3_4_58_2","doi-asserted-by":"crossref","unstructured":"J. Liu . The atomic coordinate of GPI-MT-I complex. 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