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Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS

DOI: 10.1016/j.str.2017.05.009 DOI Help

Authors: David Albesa-jove (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU); Universidad del País Vasco; IKERBASQUE) , Javier Romero-garcia (Universitat Ramon Llull) , Enea Sancho-vaello (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU)) , F.-xabier Contreras (Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU); Universidad del País Vasco; IKERBASQUE) , Ane Rodrigo-unzueta (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU)) , Natalia Comino (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU); IKERBASQUE) , Ana Carreras-gonzalez (CIC bioGUNE) , Pedro Arrasate (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU)) , Saioa Urresti (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU)) , Xevi Biarnes (Universitat Ramon Llull) , Antoni Planas (Universitat Ramon Llull) , Marcelo Guerin (CIC bioGUNE; Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU); Universidad del País Vasco; IKERBASQUE)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure

State: Published (Approved)
Published: June 2017
Diamond Proposal Number(s): 8302 , 10130

Abstract: Glycosyltransferases (GTs) play a central role in nature. They catalyze the transfer of a sugar moiety to a broad range of acceptor substrates. GTs are highly selective enzymes, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their sugar and acceptor substrates. We report here a series of structural snapshots of the reaction center of the retaining glucosyl-3-phosphoglycerate synthase (GpgS). During this sequence of events, we visualize how the enzyme guides the substrates into the reaction center where the glycosyl transfer reaction takes place, and unveil the mechanism of product release, involving multiple conformational changes not only in the substrates/products but also in the enzyme. The structural data are further complemented by metadynamics free-energy calculations, revealing how the equilibrium of loop conformations is modulated along these itineraries. The information reported here represent an important contribution for the understanding of GT enzymes at the molecular level.

Journal Keywords: enzyme catalysis; enzyme dynamics; enzyme structure; enzyme mechanism; carbohydrate biosynthesis; carbohydrate modifying enzymes; glycosyltransferases; lipopolysaccharide; mycobacteria

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: SOLEIL