Secondary structure reshuffling modulates glycosyltransferase function at the membrane.

Lien vers Pubmed [PMID] – 25402770

Lien DOI – 10.1038/nchembio.1694

Nat Chem Biol 2015 Jan; 11(1): 16-8

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.