This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fpk
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1fpk.jpg|left|200px]]<br /><applet load="1fpk" size=" | + | [[Image:1fpk.jpg|left|200px]]<br /><applet load="1fpk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fpk, resolution 3.0Å" /> | caption="1fpk, resolution 3.0Å" /> | ||
'''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH THALLIUM IONS (10 MM)'''<br /> | '''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH THALLIUM IONS (10 MM)'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1FPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with TL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Known structural/functional Sites: <scene name='pdbsite=TH1:First Metal Site In The Monomer Composed Of Chains A'>TH1</scene>, <scene name='pdbsite=TH2:First Metal Site In The Monomer Composed Of Chains B'>TH2</scene>, <scene name='pdbsite=TH3:Second Metal Site In The Monomer Composed Of Chains A'>TH3</scene>, <scene name='pdbsite=TH4:Second Metal Site In The Monomer Composed Of Chains B'>TH4</scene>, <scene name='pdbsite=TH5:Third Metal Site In The Monomer Composed Of Chains A'>TH5</scene> and <scene name='pdbsite=TH6:Third Metal Site In The Monomer Composed Of Chains B'>TH6</scene>. Full crystallographic information is available from [http:// | + | 1FPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=TL:'>TL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Known structural/functional Sites: <scene name='pdbsite=TH1:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH1</scene>, <scene name='pdbsite=TH2:First+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH2</scene>, <scene name='pdbsite=TH3:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH3</scene>, <scene name='pdbsite=TH4:Second+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH4</scene>, <scene name='pdbsite=TH5:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+A'>TH5</scene> and <scene name='pdbsite=TH6:Third+Metal+Site+In+The+Monomer+Composed+Of+Chains+B'>TH6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPK OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: phosphoric monoester]] | [[Category: phosphoric monoester]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:39:59 2008'' |
Revision as of 07:39, 3 February 2008
|
FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH THALLIUM IONS (10 MM)
Overview
Fructose-1,6-bisphosphatase (Fru-1,6-Pase; D-fructose-1,6-bisphosphate, 1-phosphohydrolase, EC 3.1.3.11) requires two divalent metal ions to, hydrolyze alpha-D-fructose 1,6-bisphosphate. Although not required for, catalysis, monovalent cations modify the enzyme activity; K+ and Tl+ ions, are activators, whereas Li+ ions are inhibitors. Their mechanisms of, action are still unknown. We report here crystallographic structures of, pig kidney Fru-1,6-Pase complexed with K+, Tl+, or both Tl+ and Li+. In, the T form Fru-1,6-Pase complexed with the substrate analogue, 2,5-anhydro-D-glucitol 1,6-bisphosphate (AhG-1,6-P2) and Tl+ or K+ ions, three Tl+ or K+ binding sites are found. Site 1 is defined by Glu-97, Asp-118, Asp-121, Glu-280, and a 1-phosphate oxygen of AhG-1,6-P2; site 2, is defined by Glu-97, Glu-98, Asp-118, and Leu-120. Finally, site 3 is, defined by Arg-276, Glu-280, and the 1-phosphate group of AhG-1,6-P2. The, Tl+ or K+ ions at sites 1 and 2 are very close to the positions previously, identified for the divalent metal ions. Site 3 is specific to K+ or Tl+., In the divalent metal ion complexes, site 3 is occupied by the guanidinium, group of Arg-276. These observations suggest that Tl+ or K+ ions can, substitute for Arg-276 in the active site and polarize the 1-phosphate, group, thus facilitating nucleophilic attack on the phosphorus center. In, the T form complexed with both Tl+ and Li+ ions, Li+ replaces Tl+ at metal, site 1. Inhibition by lithium very likely occurs as it binds to this site, thus retarding turnover or phosphate release. The present study provides a, structural basis for a similar mechanism of inhibition for inositol, monophosphatase, one of the potential targets of lithium ions in the, treatment of manic depression.
About this Structure
1FPK is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.
Reference
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase., Villeret V, Huang S, Fromm HJ, Lipscomb WN, Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8916-20. PMID:7568043
Page seeded by OCA on Sun Feb 3 09:39:59 2008
