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Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA

dc.contributor.authorAnso, Itxaso
dc.contributor.authorBasso, Luis G. M.
dc.contributor.authorWang, Lei
dc.contributor.authorMarina, Alberto
dc.contributor.authorPáez Pérez, Edgar Daniel
dc.contributor.authorJager, Christian
dc.contributor.authorGavotto, Floriane
dc.contributor.authorTersa, Montse
dc.contributor.authorPerrone, Sebastian
dc.contributor.authorContreras, F-Xabier
dc.contributor.authorPrandi, Jacques
dc.contributor.authorGilleron, Martine
dc.contributor.authorLinster, Carole L.
dc.contributor.authorCorzana, Francisco
dc.contributor.authorLowary, Todd L.
dc.contributor.authorTrastoy, Beatriz
dc.contributor.authorGuerin, Marcelo E.
dc.identifier.citationAnso, I., Basso, L. G. M., Wang, L., Marina, A., Páez-Pérez, E. D., Jäger, C., … Guerin, M. E. (2021). Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA. Science Advances, 7(42).
dc.description.abstract"Glycolipids are prominent components of bacterial membranes that play critical roles not only in maintaining the structural integrity of the cell but also in modulating host-pathogen interactions. PatA is an essential acyltransferase involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs), key structural elements and virulence factors of Mycobacterium tuberculosis. We demonstrate by electron spin resonance spectroscopy and surface plasmon resonance that PatA is an integral membrane acyltransferase tightly anchored to anionic lipid bilayers, using a two-helix structural motif and electrostatic interactions. PatA dictates the acyl chain composition of the glycolipid by using an acyl chain selectivity “ruler.” We established this by a combination of structural biology, enzymatic activity, and binding measurements on chemically synthesized nonhydrolyzable acyl–coenzyme A (CoA) derivatives. We propose an interfacial catalytic mechanism that allows PatA to acylate hydrophobic PIMs anchored in the inner membrane of mycobacteria, through the use of water-soluble acyl-CoA donors."
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.subjectBacillus-calmette guerin
dc.subjectPhosphatidylinositol mannosides
dc.subjectMannosyltransferase pima
dc.subjectEnzymatic acylation
dc.subjectStructural basis
dc.subject.classificationCIENCIAS TECNOLÓGICAS
dc.titleMolecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA
dc.rights.accessAcceso Abierto

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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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