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5k56

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Current revision (10:39, 27 September 2023) (edit) (undo)
 
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==Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate==
==Human muscle fructose-1,6-bisphosphatase in active R-state in complex with fructose-1,6-bisphosphate==
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<StructureSection load='5k56' size='340' side='right' caption='[[5k56]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='5k56' size='340' side='right'caption='[[5k56]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k56]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K56 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5k56]] 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=5K56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K56 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=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</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]] 2.198&#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]], [[5et5|5et5]], [[5et6|5et6]], [[5et7|5et7]], [[5et8|5et8]]</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=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5k56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k56 OCA], [https://pdbe.org/5k56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k56 RCSB], [https://www.ebi.ac.uk/pdbsum/5k56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k56 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k56 OCA], [http://pdbe.org/5k56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k56 RCSB], [http://www.ebi.ac.uk/pdbsum/5k56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k56 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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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 5k56" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Fructose-1%2C6-bisphosphatase|Fructose-1%2C6-bisphosphatase]]
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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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: Human]]
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[[Category: Large Structures]]
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[[Category: Barciszewski, J]]
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[[Category: Barciszewski J]]
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[[Category: Dzugaj, A]]
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[[Category: Dzugaj A]]
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[[Category: Jaskolski, M]]
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[[Category: Jaskolski M]]
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[[Category: Kolodziejczyk, R]]
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[[Category: Kolodziejczyk R]]
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[[Category: Rakus, D]]
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[[Category: Rakus D]]
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[[Category: Wisniewski, J]]
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[[Category: Wisniewski J]]
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[[Category: Carbohydrate metabolism]]
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[[Category: F16bp]]
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[[Category: Fbpase]]
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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 izozyme]]
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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-1,6-bisphosphate

PDB ID 5k56

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