7OJT

Crystal structure of unliganded PatA, a membrane associated acyltransferase from Mycobacterium smegmatis

Summary for 7OJT

• Entry DOI: 10.2210/pdb7ojt/pdb
• Descriptor: Phosphatidylinositol mannoside acyltransferase, GLYCEROL (2 entities in total)
• Functional Keywords: acyltrasnferase, mycobacteria, integral membrane protein transferase, transferase
• Biological source: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
• Total number of polymer chains: 4
• Total formula weight: 139145.45

Authors

Anso, I.,Wang, L.,Marina, A.,Paez-Perez, E.D.,Perrone, S.,Lowary, T.L.,Trastoy, B.,Guerin, M.E. (deposition date: 2021-05-17, release date: 2021-10-27, Last modification date: 2024-01-31)

Primary citation

Anso, I.,Basso, L.G.M.,Wang, L.,Marina, A.,Paez-Perez, E.D.,Jager, C.,Gavotto, F.,Tersa, M.,Perrone, S.,Contreras, F.X.,Prandi, J.,Gilleron, M.,Linster, C.L.,Corzana, F.,Lowary, T.L.,Trastoy, B.,Guerin, M.E.
Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA.
Sci Adv, 7:eabj4565-eabj4565, 2021

PubMed 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--inositol mannosides (PIMs), key structural elements and virulence factors of . 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.

PubMed: 34652941
DOI: 10.1126/sciadv.abj4565

Experimental method

X-RAY DIFFRACTION (3.67 Å)