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| | <StructureSection load='3qpu' size='340' side='right'caption='[[3qpu]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3qpu' size='340' side='right'caption='[[3qpu]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qpu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qpu]] 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=3QPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qpv|3qpv]], [[3qpw|3qpw]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFKFB3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpu OCA], [https://pdbe.org/3qpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpu RCSB], [https://www.ebi.ac.uk/pdbsum/3qpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpu ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpu OCA], [https://pdbe.org/3qpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpu RCSB], [https://www.ebi.ac.uk/pdbsum/3qpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN]] Synthesis and degradation of fructose 2,6-bisphosphate.
| + | [https://www.uniprot.org/uniprot/F263_HUMAN F263_HUMAN] Synthesis and degradation of fructose 2,6-bisphosphate. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The molecular basis of Fructose-2,6-bisphosphatase (F-2,6-P(2) ase) of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB) was investigated using the crystal structures of the human inducible form (PFKFB3) in a phospho-enzyme intermediate state (PFKFB3-P*F-6-P), in a transition state-analogous complex (PFKFB3*AlF4), and in a complex with pyrophosphate (PFKFB3*PP(i) ) at resolutions of 2.45A, 2.2A, and 2.3A, respectively. Trapping the PFKFB3-P*F-6-P intermediate was achieved by flash cooling the crystal during the reaction, and the PFKFB3*AlF4 and PFKFB3*PP(i) complexes were obtained by soaking. The PFKFB3*AlF(4) and PFKFB3*PP(i) complexes resulted in removing F-6-P from the catalytic pocket. With these structures, the structures of the Michaelis complex and the transition state were extrapolated. For both the PFKFB3-P formation and break down, the phosphoryl donor and the acceptor are located within approximately 5.1A, and the pivotal point 2-P is on the same line, suggesting an "in-line" transfer with a direct inversion of phosphate configuration. The geometry suggests that NE2 of His253 undergoes a nucleophilic attack to form a covalent N-P bond, breaking the 2O-P bond in the substrate. The resulting high reactivity of the leaving group, 2O of F-6-P, is neutralized by a proton donated by Glu322. Negative charges on the equatorial oxygens of the transient bipyramidal phosphorane formed during the transfer are stabilized by Arg252, His387, and Asn259. The C-terminal domain (residues 440-446) was rearranged in PFKFB3*PP(i) , implying that this domain plays a critical role in binding of substrate to and release of product from the F-2,6-P(2) ase catalytic pocket. These findings provide a new insight into the understanding of the phosphoryl transfer reaction. Proteins 2011. (c) 2011 Wiley-Liss, Inc.
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| - | Molecular basis of the Fructose-2,6-bisphosphatase reaction of PFKFB3: Transition state and the C-terminal function.,Cavalier MC, Kim SG, Neau D, Lee YH Proteins. 2011 Dec 21. doi: 10.1002/prot.24015. PMID:22275052<ref>PMID:22275052</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3qpu" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cavalier, M C]] | + | [[Category: Cavalier MC]] |
| - | [[Category: Kim, S G]] | + | [[Category: Kim SG]] |
| - | [[Category: Lee, Y H]] | + | [[Category: Lee YH]] |
| - | [[Category: Neau, D]] | + | [[Category: Neau D]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Kinase/bisphosphatase]]
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| - | [[Category: Transferase]]
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