5et8

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==Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-6-phosphate==
==Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-6-phosphate==
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<StructureSection load='5et8' size='340' side='right' caption='[[5et8]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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<StructureSection load='5et8' size='340' side='right'caption='[[5et8]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5et8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ET8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ET8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5et8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ET8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ET8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ifa|3ifa]], [[3ifc|3ifc]], [[4he0|4he0]], [[4he1|4he1]], [[4he2|4he2]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5et8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5et8 OCA], [https://pdbe.org/5et8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5et8 RCSB], [https://www.ebi.ac.uk/pdbsum/5et8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5et8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5et8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5et8 OCA], [http://pdbe.org/5et8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5et8 RCSB], [http://www.ebi.ac.uk/pdbsum/5et8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5et8 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F16P2_HUMAN F16P2_HUMAN]
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Human fructose-1,6-bisphosphatase is an allosteric enzyme that is regulated by different ligands. There are only two known isozymes in human tissues: the liver isozyme (the key enzyme of gluconeogenesis), which is regulated by fructose 2,6-bisphosphate, and its muscle counterpart (participating in glycogen synthesis), which is regulated by calcium ions. AMP, which is an allosteric inhibitor of both isozymes, inhibits the muscle isozyme with an I(0.5) that is 35-100 times lower than for the liver isozyme and the reason for this difference remains obscure. In studies aiming at an explanation of the main differences in the regulation of the two isozymes, it has been shown that only one residue, in position 69, regulates the sensitivity towards calcium ions. As a consequence of this finding, an E69Q mutant of the muscle isozyme, which is insensitive to calcium ions while retaining all other kinetic properties resembling the liver isozyme, has been prepared and crystallized. Here, two crystal structures of this mutant enzyme in complex with AMP with and without fructose 6-phosphate (the product of the catalytic reaction) are presented. The AMP binding pattern of the muscle isozyme is quite similar to that of the liver isozyme and the T conformations of the two isozymes are nearly the same.
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Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.,Zarzycki M, Kolodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1028-34. doi:, 10.1107/S090744491104385X. Epub 2011 Nov 18. PMID:22120740<ref>PMID:22120740</ref>
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==See Also==
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5et8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fructose-bisphosphatase]]
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[[Category: Homo sapiens]]
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[[Category: Barciszewski, J]]
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[[Category: Large Structures]]
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[[Category: Dzugaj, A]]
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[[Category: Barciszewski J]]
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[[Category: Jaskolski, M]]
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[[Category: Dzugaj A]]
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[[Category: Kolodziejczyk, R]]
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[[Category: Jaskolski M]]
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[[Category: Rakus, D]]
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[[Category: Kolodziejczyk R]]
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[[Category: Wisniewski, J]]
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[[Category: Rakus D]]
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[[Category: Asp187]]
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[[Category: Wisniewski J]]
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[[Category: Carbohydrate metabolism]]
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[[Category: Fbpase]]
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[[Category: Fructose-6-phosphate]]
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[[Category: Glyconeogenesis]]
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[[Category: Hydrolase]]
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[[Category: Leucine lock]]
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[[Category: Muscle]]
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[[Category: R-state]]
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Current revision

Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-6-phosphate

PDB ID 5et8

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