1yp2
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1yp2.gif|left|200px]]<br /><applet load="1yp2" size=" | + | [[Image:1yp2.gif|left|200px]]<br /><applet load="1yp2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yp2, resolution 2.11Å" /> | caption="1yp2, resolution 2.11Å" /> | ||
'''Crystal structure of potato tuber ADP-glucose pyrophosphorylase'''<br /> | '''Crystal structure of potato tuber ADP-glucose pyrophosphorylase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ADP-glucose pyrophosphorylase catalyzes the first committed and | + | 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== | ==About this Structure== | ||
| - | 1YP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum] with SO4 and PMB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_adenylyltransferase Glucose-1-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.27 2.7.7.27] Full crystallographic information is available from [http:// | + | 1YP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PMB:'>PMB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_adenylyltransferase Glucose-1-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.27 2.7.7.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP2 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Solanum tuberosum]] | [[Category: Solanum tuberosum]] | ||
| - | [[Category: Ballicora, M | + | [[Category: Ballicora, M A.]] |
| - | [[Category: Geiger, J | + | [[Category: Geiger, J H.]] |
[[Category: Jin, X.]] | [[Category: Jin, X.]] | ||
[[Category: Preiss, J.]] | [[Category: Preiss, J.]] | ||
| Line 25: | Line 25: | ||
[[Category: alpha-d-glucose-1-phosphate adenyl transferase]] | [[Category: alpha-d-glucose-1-phosphate adenyl transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:35 2008'' |
Revision as of 14:07, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 16:07:35 2008
