View source for 3qpw


==PFKFB3 in complex with Aluminum Tetrafluoride==
<StructureSection load='3qpw' size='340' side='right'caption='[[3qpw]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qpw]] 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=3QPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene></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=3qpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpw OCA], [https://pdbe.org/3qpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpw RCSB], [https://www.ebi.ac.uk/pdbsum/3qpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpw ProSAT]</span></td></tr>
</table>
== Function ==
[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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qpw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cavalier MC]]
[[Category: Kim SG]]
[[Category: Lee YH]]
[[Category: Neau D]]