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Deciphering the Molecular Mechanism of an Enzymatic Machinery for Glycogen Biosynthesis

Project description

Investigating the molecular machinery of glycogenesis

Glycogen is a branched polysaccharide that represents the main storage form of glucose in organisms and serves as an energy source in animals, fungi and bacteria. The Glycogenin 1 (GYG1) enzyme converts glucose to glycogen, acting in the initial polymerisation of the glucose molecules, after which other enzymes take over. Funded by the Marie Skłodowska-Curie Actions programme, the DeciphGYG project aims to design a new approach to investigate the mechanisms of glycogen biosynthesis, combining computational modelling with experimental data from crystallography and nuclear magnetic resonance. The objective is to fully understand the mechanism of human GYG1 action to facilitate drug design against glycogen storage disease type XV caused by the enzyme T83M variant.

Objective

The biosynthesis of glycogen - glycogenesis - represents a key glucose (and hence energy) storage process across a wide range of organisms. Human glycogenin 1 (hGYG1) is one of the two primary enzymes that initiates the biosynthesis of glycogen, our energy reservoir. It polymerizes a maltosaccharide chain covalently attached to an enzyme residue, Y195, via a stepwise glycosylation reaction. In the reaction cycle, a dynamic conformational switch between ground and active states induced by one of the enzyme substrates, the sugar donor UDP-glucose, was predicted by structural studies, including a stretch of a critical loop containing Y195, the acceptor arm, and a major movement of a 32-residue lid covering the active site. The T83M mutation, which causes glycogen storage disease (GSD) type XV, makes the enzyme catalytically inactive. The scientific aim of DeciphGYG is to design a new protocol combining a series of both computational techniques (MD, QM/MM MetaD, HREX and BE-MetaD) and experimental results (NMR and crystallography) to unveil the mechanisms of glycogen biosynthesis, including both the glycosylation reaction as well as its coupling with the conformational changes induced by binding of the UDP-glucose donor and acceptor substrates. The experienced researcher (ER), Qinghua Liao will carry out the project in the University of Barcelona under the supervision of Prof. Carme Rovira, who has extensive experience in computational modeling of carbohydrate-active enzymes. Our goal will be shaping the understanding of hGYG1 action fully on glycogen biosynthesis, facilitating drug design against GSD type XV. Moreover, the new protocol will be transferable to other enzymes of interest in glycobiology. Altogether, the DeciphGYG project will allow the ER with a highly competitive multidisciplinary profile by complementing his previous acquired skills, placing him at a strong position to start his career as an independent and innovative principal investigator.

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MSCA-IF - Marie Skłodowska-Curie Individual Fellowships (IF)

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Call for proposal

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(opens in new window) H2020-MSCA-IF-2020

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Coordinator

UNIVERSITAT DE BARCELONA
Net EU contribution

Net EU financial contribution. The sum of money that the participant receives, deducted by the EU contribution to its linked third party. It considers the distribution of the EU financial contribution between direct beneficiaries of the project and other types of participants, like third-party participants.

€ 172 932,48
Address
GRAN VIA DE LES CORTS CATALANES 585
08007 BARCELONA
Spain

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Region
Este Cataluña Barcelona
Activity type
Higher or Secondary Education Establishments
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Total cost

The total costs incurred by this organisation to participate in the project, including direct and indirect costs. This amount is a subset of the overall project budget.

€ 172 932,48
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