1fpl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1fpl.jpg|left|200px]] | [[Image:1fpl.jpg|left|200px]] | ||
'''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND THALLIUM IONS (10 MM)''' | {{Structure | ||
|PDB= 1fpl |SIZE=350|CAPTION= <scene name='initialview01'>1fpl</scene>, resolution 2.3Å | |||
|SITE= <scene name='pdbsite=AC1:Active+Site+In+The+Monomer+Composed+Of+Chains+A'>AC1</scene>, <scene name='pdbsite=AC2:Active+Site+In+The+Monomer+Composed+Of+Chains+B'>AC2</scene>, <scene name='pdbsite=AM1:Amp+Binding+Site+In+The+Monomer+Composed+Of+Chains+A'>AM1</scene>, <scene name='pdbsite=AM2:Amp+Binding+Site+In+The+Monomer+Composed+Of+Chains+B'>AM2</scene>, <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> | |||
|LIGAND= <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=AHG:2,5-ANHYDROGLUCITOL-1,6-BIPHOSPHATE'>AHG</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND THALLIUM IONS (10 MM)''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1FPL is a [ | 1FPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPL OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7568043 7568043] | ||
[[Category: Fructose-bisphosphatase]] | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 32: | ||
[[Category: phosphoric monoester]] | [[Category: phosphoric monoester]] | ||
''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 11:12:18 2008'' | ||
Revision as of 12:12, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | , and | ||||||
| Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND THALLIUM IONS (10 MM)
OverviewOverview
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 StructureAbout this Structure
1FPL is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 11:12:18 2008