Reference : Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltran...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/48624
Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA
English
Anso, Itxaso [> >]
Basso, Luis G. M. [> >]
Wang, Lei [> >]
Marina, Alberto [> >]
Páez-Pérez, Edgar D. [> >]
Jäger, Christian mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > Scientific Central Services]
gavotto, Floriane mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > Scientific Central Services >]
Tersa, Montse [> >]
Perrone, Sebastian mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > Enzymology and Metabolism >]
Contreras, F.-Xabier [> >]
Prandi, Jacques [> >]
Gilleron, Martine [> >]
Linster, Carole mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > Enzymology and Metabolism >]
Corzana, Francisco [> >]
Lowary, Todd L. [> >]
Trastoy, Beatriz [> >]
Guerin, Marcelo E. [> >]
2021
Science Advances
7
42
Yes (verified by ORBilu)
International
2375-2548
[en] 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.
http://hdl.handle.net/10993/48624
10.1126/sciadv.abj4565
https://www.science.org/doi/10.1126/sciadv.abj4565

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