2g50
From Proteopedia
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| - | [[Image:2g50.gif|left|200px]] | + | [[Image:2g50.gif|left|200px]] |
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| - | '''The location of the allosteric amino acid binding site of muscle pyruvate kinase.''' | + | {{Structure |
| + | |PDB= 2g50 |SIZE=350|CAPTION= <scene name='initialview01'>2g50</scene>, resolution 1.650Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The location of the allosteric amino acid binding site of muscle pyruvate kinase.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G50 is a [ | + | 2G50 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G50 OCA]. |
==Reference== | ==Reference== | ||
| - | Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase., Williams R, Holyoak T, McDonald G, Gui C, Fenton AW, Biochemistry. 2006 May 2;45(17):5421-9. PMID:[http:// | + | Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase., Williams R, Holyoak T, McDonald G, Gui C, Fenton AW, Biochemistry. 2006 May 2;45(17):5421-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16634623 16634623] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Pyruvate kinase]] | [[Category: Pyruvate kinase]] | ||
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[[Category: pyruvate kinase]] | [[Category: pyruvate kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:00:31 2008'' |
Revision as of 15:00, 20 March 2008
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| , resolution 1.650Å | |||||||
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| Ligands: | , , , , , , and | ||||||
| Activity: | Pyruvate kinase, with EC number 2.7.1.40 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The location of the allosteric amino acid binding site of muscle pyruvate kinase.
Overview
The isoform of pyruvate kinase from brain and muscle of mammals (M(1)-PYK) is allosterically inhibited by phenylalanine. Initial observations in this model allosteric system indicate that Ala binds competitively with Phe, but elicits a minimal allosteric response. Thus, the allosteric ligand of this system must have requirements for eliciting an allosteric response in addition to the requirements for binding. Phe analogues have been used to dissect what chemical properties of Phe are responsible for eliciting the allosteric response. We first demonstrate that the l-2-aminopropanaldehyde substructure of the amino acid ligand is primarily responsible for binding to M(1)-PYK. Since the allosteric response to Ala is minimal and linear addition of methyl groups beyond the beta-carbon increase the magnitude of the allosteric response, we conclude that moieties beyond the beta-carbon are primarily responsible for allostery. Instead of an all-or-none mechanism of allostery, these findings support the idea that the bulk of the hydrophobic side chain, but not the aromatic nature, is the primary determinant of the magnitude of the observed allosteric inhibition. The use of these results to direct structural studies has resulted in a 1.65 A structure of M(1)-PYK with Ala bound. The coordination of Ala in the allosteric amino acid binding site confirms the binding role of the l-2-aminopropanaldehyde substructure of the ligand. Collectively, this study confirms that a ligand can have chemical regions specific for eliciting the allosteric signal in addition to the chemical regions necessary for binding.
About this Structure
2G50 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase., Williams R, Holyoak T, McDonald G, Gui C, Fenton AW, Biochemistry. 2006 May 2;45(17):5421-9. PMID:16634623
Page seeded by OCA on Thu Mar 20 17:00:31 2008
Categories: Oryctolagus cuniculus | Pyruvate kinase | Single protein | Fenton, A W. | Holyoak, T. | Williams, R. | ALA | EDO | ETE | GOL | K | MN | NA | PYR | Allostery | Glycolysis | Kinase | Phosphoryl transfer
