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

AuthorsAlbesa-Jové, David; Rodrigo-Unzueta, Ane; Gomollón-Bel, Fernando CSIC ORCID; Cifuente, Javier O.; Urresti, Saioa; Comino, Natalia; Sancho-Vaello, Enea CSIC ORCID; Merino, Pedro CSIC ORCID ; 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.
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