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Secondary structure reshuffling modulates glycosyltransferase function at the membrane

DOI: 10.1038/nchembio.1694 DOI Help

Authors: David Giganti (Institut Pasteur) , David Albesa-jove (Unit of Biophysics) , Saioa Urresti (Unidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Científicas-Universidad del País Vasco/Euskal Herriko Unibertsitatea, Spain) , Ane Rodrigo-unzueta (Centro Mixto Consejo Superior de Investigaciones Cientificas–Universidad del País Vasco/Euskal Herriko Unibertsitatea) , Mariano A Martínez (Institut Pasteur) , Natalia Comino (Unidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Científicas-Universidad del País Vasco/Euskal Herriko Unibertsitatea, Spain) , Nathalie Barilone (Institut Pasteur) , Marco Bellinzoni (Institut Pasteur) , Alexandre Chenal (Institut Pasteur) , Marcelo Guerin (Unit of Biophysics) , Pedro M Alzari (Institut Pasteur)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemical Biology , VOL 11 (1) , PAGES 16 - 18

State: Published (Approved)
Published: November 2014
Diamond Proposal Number(s): 8302 , 10130

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 beta-strand–to–alpha-helix and alpha-helix–to–beta-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography

Other Facilities: SOLEIL BEAMLINE PROXIMA 1