Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.

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Bibliographic Details
Title: Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.
Authors: Low YS; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia., Roche SG; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia., Aleksandrova NA; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia., Foley G; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia., Low JK; School of Life and Environmental Sciences, University of Sydney, Camperdown, NSW, Australia., Box JK; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia., Croll TI; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.; Altos Labs, Cambridge, UK., Chassagnon IR; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia.; Servatus Biopharmaceuticals, Coolum Beach, QLD, Australia., Lott JS; School of Biological Sciences, University of Auckland, Auckland, New Zealand., Deplazes E; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia., Bodén M; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia., Hurst MR; Bioeconomy Science Institute, AgResearch, Lincoln Research Centre, Christchurch, New Zealand., Piper SJ; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia. sarah.piper@monash.edu.au.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia. sarah.piper@monash.edu.au.; Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia. sarah.piper@monash.edu.au.; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD, Australia. sarah.piper@monash.edu.au., Landsberg MJ; School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, Australia. m.landsberg@uq.edu.au.; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia. m.landsberg@uq.edu.au.; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD, Australia. m.landsberg@uq.edu.au.
Source: Nature communications [Nat Commun] 2025 Dec 15; Vol. 16 (1), pp. 11121. Date of Electronic Publication: 2025 Dec 15.
Publication Type: Journal Article
Journal Info: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Database: MEDLINE Ultimate
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