1bq3
From Proteopedia
(New page: 200px<br /><applet load="1bq3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bq3, resolution 2.7Å" /> '''SACCHAROMYCES CEREVIS...) |
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| - | [[Image:1bq3.jpg|left|200px]]<br /><applet load="1bq3" size=" | + | [[Image:1bq3.jpg|left|200px]]<br /><applet load="1bq3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bq3, resolution 2.7Å" /> | caption="1bq3, resolution 2.7Å" /> | ||
'''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE'''<br /> | '''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The effects that the inhibitors inositol hexakisphosphate and benzene | + | The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1BQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and IHP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http:// | + | 1BQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=IHP:'>IHP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQ3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fothergill-Gilmore, L | + | [[Category: Fothergill-Gilmore, L A.]] |
| - | [[Category: Phillips, S | + | [[Category: Phillips, S E.V.]] |
| - | [[Category: Rigden, D | + | [[Category: Rigden, D J.]] |
[[Category: IHP]] | [[Category: IHP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: transferase (phosphoryl)]] | [[Category: transferase (phosphoryl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:50 2008'' |
Revision as of 09:57, 21 February 2008
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SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE
Overview
The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis.
About this Structure
1BQ3 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Full crystallographic information is available from OCA.
Reference
Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis., Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA, J Mol Biol. 1999 Jun 18;289(4):691-9. PMID:10369755
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