1yp2
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(New page: 200px<br /><applet load="1yp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yp2, resolution 2.11Å" /> '''Crystal structure of...)
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Revision as of 04:50, 21 November 2007
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Crystal structure of potato tuber ADP-glucose pyrophosphorylase
Overview
ADP-glucose pyrophosphorylase catalyzes the first committed and, rate-limiting step in starch biosynthesis in plants and glycogen, biosynthesis in bacteria. It is the enzymatic site for regulation of, storage polysaccharide accumulation in plants and bacteria, being, allosterically activated or inhibited by metabolites of energy flux. We, report the first atomic resolution structure of ADP-glucose, pyrophosphorylase. Crystals of potato tuber ADP-glucose pyrophosphorylase, alpha subunit were grown in high concentrations of sulfate, resulting in, the sulfate-bound, allosterically inhibited form of the enzyme. The, N-terminal catalytic domain resembles a dinucleotide-binding Rossmann fold, and the C-terminal domain adopts a left-handed parallel beta helix that is, involved in cooperative allosteric regulation and a unique, oligomerization. We also report structures of the enzyme in complex with, ATP and ADP-glucose. Communication between the regulator-binding sites and, the active site is both subtle and complex and involves several distinct, regions of the enzyme including the N-terminus, the, glucose-1-phosphate-binding site, and the ATP-binding site. These, structures provide insights into the mechanism for catalysis and, allosteric regulation of the enzyme.
About this Structure
1YP2 is a Single protein structure of sequence from Solanum tuberosum with SO4 and PMB as ligands. Active as Glucose-1-phosphate adenylyltransferase, with EC number 2.7.7.27 Full crystallographic information is available from OCA.
Reference
Crystal structure of potato tuber ADP-glucose pyrophosphorylase., Jin X, Ballicora MA, Preiss J, Geiger JH, EMBO J. 2005 Feb 23;24(4):694-704. Epub 2005 Feb 3. PMID:15692569
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