1RZV

Crystal structure of the glycogen synthase from Agrobacterium tumefaciens (non-complexed form)

Summary for 1RZV

• Entry DOI: 10.2210/pdb1rzv/pdb
• Related: 1rzu
• Descriptor: Glycogen synthase 1 (2 entities in total)
• Functional Keywords: glycosyl-transferase gt-b fold, rossmann fold, transferase
• Biological source: Agrobacterium tumefaciens
• Total number of polymer chains: 2
• Total formula weight: 105851.47

Authors

Buschiazzo, A.,Guerin, M.E.,Ugalde, J.E.,Ugalde, R.A.,Shepard, W.,Alzari, P.M. (deposition date: 2003-12-29, release date: 2004-08-31, Last modification date: 2024-10-30)

Primary citation

Buschiazzo, A.,Ugalde, J.E.,Guerin, M.E.,Shepard, W.,Ugalde, R.A.,Alzari, P.M.
Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation.
Embo J., 23:3196-3205, 2004

PubMed Abstract: Glycogen and starch are the major readily accessible energy storage compounds in nearly all living organisms. Glycogen is a very large branched glucose homopolymer containing about 90% alpha-1,4-glucosidic linkages and 10% alpha-1,6 linkages. Its synthesis and degradation constitute central pathways in the metabolism of living cells regulating a global carbon/energy buffer compartment. Glycogen biosynthesis involves the action of several enzymes among which glycogen synthase catalyzes the synthesis of the alpha-1,4-glucose backbone. We now report the first crystal structure of glycogen synthase in the presence and absence of adenosine diphosphate. The overall fold and the active site architecture of the protein are remarkably similar to those of glycogen phosphorylase, indicating a common catalytic mechanism and comparable substrate-binding properties. In contrast to glycogen phosphorylase, glycogen synthase has a much wider catalytic cleft, which is predicted to undergo an important interdomain 'closure' movement during the catalytic cycle. The structures also provide useful hints to shed light on the allosteric regulation mechanisms of yeast/mammalian glycogen synthases.

PubMed: 15272305
DOI: 10.1038/sj.emboj.7600324

Experimental method

X-RAY DIFFRACTION (2.3 Å)