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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Acta crystallographica. Section D, Biological crystallography

Preliminary crystallographic studies of glycogen synthase from Agrobacterium tumefaciens

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section D, Biological crystallography - 21 Feb 2003

Guerin ME, Buschiazzo A, Ugalde JE, Ugalde RA, Alzari PM

Link to Pubmed [PMID] – 12595715

Acta Crystallogr. D Biol. Crystallogr. 2003 Mar;59(Pt 3):526-8

Crystals of the glycogen synthase (GS) from Agrobacterium tumefaciens have been grown that diffract to 2.6 A resolution. The enzyme, which is homologous to the starch synthases of plants, catalyzes the last reaction step in the biosynthesis of glycogen. It is a alpha-retaining glucosyltransferase that uses ADP-glucose to incorporate additional glucose monomers onto the growing glycogen polymer. Its homology with mammalian GSs is marginal, but several regions shown to be important in catalysis are strictly conserved. Knowledge of the crystal structure of GS will be a major advance in the understanding of glycogen/starch metabolism and its regulation. A rational approach in enzyme engineering can subsequently be envisaged. The multiwavelength anomalous diffraction approach will be used to solve the phase problem.

http://www.ncbi.nlm.nih.gov/pubmed/12595715