1pyg: Difference between revisions
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|PDB= 1pyg |SIZE=350|CAPTION= <scene name='initialview01'>1pyg</scene>, resolution 2.87Å | |PDB= 1pyg |SIZE=350|CAPTION= <scene name='initialview01'>1pyg</scene>, resolution 2.87Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=PDP:PYRIDOXAL-5 | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=PDP:PYRIDOXAL-5'-DIPHOSPHATE'>PDP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] | ||
|GENE= | |GENE= | ||
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[[Category: glycogen phosphorylase]] | [[Category: glycogen phosphorylase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:16:14 2008'' | ||
Revision as of 14:16, 23 March 2008
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| , resolution 2.87Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Phosphorylase, with EC number 2.4.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE
OverviewOverview
The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.
About this StructureAbout this Structure
1PYG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate., Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB, Science. 1991 Nov 29;254(5036):1367-71. PMID:1962195
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