Secondary structure reshuffling modulates glycosyltransferase function at the membrane

November 17th, 2014 by David Giganti

Nature Chemical Biology 11, 16 (2015). doi:10.1038/nchembio.1694

Authors: David Giganti, David Albesa-Jové, Saioa Urresti, Ane Rodrigo-Unzueta, Mariano A Martínez, Natalia Comino, Nathalie Barilone, Marco Bellinzoni, Alexandre Chenal, Marcelo E Guerin & Pedro M Alzari

Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand–to–α-helix and α-helix–to–β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.

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