English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/122607
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


A native ternary complex trapped in crystal reveals the catalytic mechanism of a retaining glycosyltransferase

AuthorsAlbesa-Jové, David; Rodrigo-Unzueta, Ane; Gomollón-Bel, Fernando ; Cifuente, Javier O.; Urresti, Saioa; Comino, Natalia; Sancho-Vaello, Enea ; Merino, Pedro ; Guerin, Marcelo E.
Structure elucidation
Issue Date2015
CitationAngewandte Chemie International Edition 54(34): 9898-9902 (2015)
AbstractGlycosyltransferases (GTs) comprise a prominent family of enzymes that play critical roles in a variety of cellular processes including cell signaling, cell development and host-pathogen interactions. Glycosyl transfer can proceed with either ‘inversion’ or ‘retention’ of the anomeric configuration with respect to the reaction substrates and products. The elucidation of the catalytic mechanism of retaining GTs remains a major challenge. We report the first native ternary complex of a GT, that of the retaining glucosyl-3-phosphoglycerate synthase GpgS from Mycobacterium tuberculosis, in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate and the divalent cation cofactor, in a productive mode for catalysis. In combination with structural, chemical, enzymatic, molecular dynamics and quantum-mechanics/molecular-mechanics (QM/MM) calculations, we unravel its catalytic mechanism, providing a strong experimental support for a front-side, substrate assisted SNi-type reaction.
Descriptionet al.
Publisher version (URL)https://doi.org/10.1002/anie.201504617
Appears in Collections:(UBF) Artículos
(ISQCH) Artículos
Files in This Item:
File Description SizeFormat 
Glycosyltransferasepost.pdf2,53 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.