J. Bailey
Trinity College, Dublin
4 Papers
J. Bailey is an academic researcher from Trinity College, Dublin. The author has contributed to research in topics: Signal peptide & Membrane protein. The author has an hindex of 4, co-authored 4 publications.
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Papers
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
TL;DR: The structure and mutagenesis studies reveal how LspA processes substrate lipoproteins and indicate that globomycin inhibits the enzyme by binding to the active site and these findings should be useful in the development of new antibiotics.
Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin.
Samir Olatunji,Xiaoxiao Yu,J. Bailey,Chia-Ying Huang,Marta Zapotoczna,Katherine Bowen,Maja Remškar,Rolf Müller,Eoin M. Scanlan,Joan A. Geoghegan,Vincent Olieric,Martin Caffrey +11 more
TL;DR: High-resolution crystal structures of the enzyme from the human pathogen methicillin-resistant Staphylococcus aureus, LspA, complexed with globomycin and with myxovirescin are provided, revealing an instance of convergent evolution.
Membrane (and Soluble) Protein Stability and Binding Measurements in the Lipid Cubic Phase Using Label-Free Differential Scanning Fluorimetry
Coilin Boland,Samir Olatunji,J. Bailey,Nicole Howe,Dietmar Weichert,Susan Kathleen Fetics,Xiaoxiao Yu,Javier Merino-Gracia,Clement Delsaut,Martin Caffrey +9 more
TL;DR: Label-free differential scanning fluorimetry should prove useful as an analytical tool for identifying host and additive lipids, detergents, precipitants and chemical probes that support the generation of quality crystals by the cubic phase method.
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Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis
Maciej Wiktor,Maciej Wiktor,Dietmar Weichert,Nicole Howe,Chia-Ying Huang,Chia-Ying Huang,Vincent Olieric,Coilin Boland,J. Bailey,L. Vogeley,Phillip J. Stansfeld,Nienke Buddelmeijer,Meitian Wang,Martin Caffrey +13 more
TL;DR: The crystal structure of the last enzyme in the pathway, apolipoprotein N-acyltransferase, Lnt, responsible for adding a third acyl chain to the lipoprotein’s invariant diacylated N-terminal cysteine is reported, suggesting plausible routes by which substrates and products enter and leave the active site.