UPV/EHU - Universidad del Pais Vasco / Euskal Herriko Unibertsitatea [Espagne] (Barrio Sarriena s/n, 48940 Leioa, Bizkaia
Campus d'Álava : Vice-Rectorado, San Antonio 41, 01005 Vitoria ;
campus de Biscaye et services centraux : Apdo 1397, 48080 Bilbao ;
campus de Guipúzcoa : Vice-Rectorado, Fuenterrabia 13-1° , 20006 San Sebastián - Spain)
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 Contributor : Bénédicte BENEDICConnect in order to contact the contributor Submitted on : Monday, December 5, 2016 - 2:05:11 PM Last modification on : Thursday, May 19, 2022 - 12:52:02 PM Long-term archiving on: : Monday, March 20, 2017 - 11:28:36 PM
File
Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed
until : jamais
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⟩