PDBsum entry 5jsx

Transferase

PDB id: 5jsx

Contents

Protein chain

282 a.a.

Ligands

UPG

GOL

Metals

_MN

Waters ×42

PDB id:

5jsx

Name:

Transferase

Title:

Crystal structure of glucosyl-3-phosphoglycerate synthase from mycobacterium tuberculosis in complex with mn2+ and uridine- diphosphate-glucose (udp-glc)

Structure:

Glucosyl-3-phosphoglycerate synthase. Chain: a. Engineered: yes

Source:

Mycobacterium tuberculosis h37ra. Organism_taxid: 419947. Gene: mra_1217. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.81Å R-factor: 0.191 R-free: 0.217

Authors:

D.Albesa-Jove,E.Sancho-Vaello,A.Rodrigo-Unzueta,N.Comino,A.Carreras- Gonzalez,P.Arrasate,S.Urresti,M.E.Guerin

Key ref:

D.Albesa-Jové et al. (2017). Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS. Structure, 25, 1034. PubMed id: 28625787 DOI: 10.1016/j.str.2017.05.009

Date:

09-May-16 Release date: 24-May-17

Protein chain

A5U1Q6  (A5U1Q6_MYCTA) -  Glycosyltransferase 2-like domain-containing protein from Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

Seq: 324 a.a.

Struc: 282 a.a.

DOI no: 10.1016/j.str.2017.05.009

Structure 25:1034 (2017)

PubMed id: 28625787

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

D.Albesa-Jové, J.Romero-García, E.Sancho-Vaello, F.X.Contreras, A.Rodrigo-Unzueta, N.Comino, A.Carreras-González, P.Arrasate, S.Urresti, X.Biarnés, A.Planas, M.E.Guerin.

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.