5JSX

Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+ and uridine-diphosphate-glucose (UDP-Glc)

Summary for 5JSX

• Entry DOI: 10.2210/pdb5jsx/pdb
• Related: 5JQX
• Descriptor: glucosyl-3-phosphoglycerate synthase, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-GLUCOSE, ... (5 entities in total)
• Functional Keywords: transferase
• Biological source: Mycobacterium tuberculosis H37Ra
• Total number of polymer chains: 1
• Total formula weight: 35396.89

Authors

Albesa-Jove, D.,Sancho-Vaello, E.,Rodrigo-Unzueta, A.,Comino, N.,Carreras-Gonzalez, A.,Arrasate, P.,Urresti, S.,Guerin, M.E. (deposition date: 2016-05-09, release date: 2017-05-24, Last modification date: 2024-01-10)

Primary citation

Albesa-Jove, D.,Romero-Garcia, J.,Sancho-Vaello, E.,Contreras, F.X.,Rodrigo-Unzueta, A.,Comino, N.,Carreras-Gonzalez, A.,Arrasate, P.,Urresti, S.,Biarnes, X.,Planas, A.,Guerin, M.E.
Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS.
Structure, 25:1034-1044.e3, 2017

PubMed 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.

PubMed: 28625787
DOI: 10.1016/j.str.2017.05.009

Experimental method

X-RAY DIFFRACTION (2.81 Å)