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1fpj
From Proteopedia
(New page: 200px<br /> <applet load="1fpj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpj, resolution 2.2Å" /> '''FRUCTOSE-1,6-BISPHOS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1FPJ 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, AMP and AHG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FPJ OCA]]. | + | 1FPJ 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, AMP and AHG as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Sites: AC1, AC2, AM1, AM2, TH3, TH4, TH5 and TH6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FPJ 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7568043 7568043] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7568043 7568043] | ||
| + | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: phosphoric monoester]] | [[Category: phosphoric monoester]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:51:03 2007'' |
Revision as of 10:46, 30 October 2007
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FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE, THALLIUM (10 MM) AND LITHIUM 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 ... [(full description)]
About this Structure
1FPJ is a [Single protein] structure of sequence from [Sus scrofa] with TL, AMP and AHG as [ligands]. Active as [Fructose-bisphosphatase], with EC number [3.1.3.11]. Structure known Active Sites: AC1, AC2, AM1, AM2, TH3, TH4, TH5 and TH6. 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
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