Abstract : 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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-01408804
Contributeur : Bénédicte Benedic
<>
Soumis le : lundi 5 décembre 2016 - 14:05:11
Dernière modification le : samedi 4 août 2018 - 01:08:35
Document(s) archivé(s) le : lundi 20 mars 2017 - 23:28:36
David Giganti, David Albesa-Jové, Saioa Urresti, Ane Rodrigo-Unzueta, Mariano A Martínez, et al.. Secondary structure reshuffling modulates glycosyltransferase function at the membrane. Nature Chemical Biology, Nature Publishing Group, 2014, 11 (1), pp.16 - 18. 〈10.1038/nchembio.1694〉. 〈pasteur-01408804〉
