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4rh3

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==AMPPCP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II==
==AMPPCP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II==
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<StructureSection load='4rh3' size='340' side='right' caption='[[4rh3]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
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<StructureSection load='4rh3' size='340' side='right'caption='[[4rh3]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rh3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RH3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rh3]] is a 4 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=4RH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RH3 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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3.02&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4omt|4omt]], [[4wlo|4wlo]], [[4u1r|4u1r]], [[4xz2|4xz2]], [[3opy|3opy]]</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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </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=4rh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh3 OCA], [https://pdbe.org/4rh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4rh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rh3 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=4rh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rh3 RCSB], [http://www.ebi.ac.uk/pdbsum/4rh3 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PFKAP_HUMAN PFKAP_HUMAN]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
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[https://www.uniprot.org/uniprot/PFKAP_HUMAN PFKAP_HUMAN] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phosphofructokinase-1 (Pfk) acts as the main control point of flux through glycolysis. It is involved in complex allosteric regulation and Pfk mutations have been linked to cancer development. Whereas the 3D structure and structural basis of allosteric regulation of prokaryotic Pfk has been studied in great detail, our knowledge about the molecular basis of the allosteric behaviour of the more complex mammalian Pfk is still very limited. To characterize the structural basis of allosteric regulation, the subunit interfaces and the functional consequences of modifications in Tarui's disease and cancer, we analysed the physiological homotetramer of human platelet Pfk at up to 2.67 A resolution in two crystal forms. The crystallized enzyme is permanently activated by a deletion of the 22 C-terminal residues. Complex structures with ADP and fructose-6-phosphate (F6P) and with ATP suggest a role of three aspartates in the deprotonation of the OH-nucleophile of F6P and in the co-ordination of the catalytic magnesium ion. Changes at the dimer interface, including an asymmetry observed in both crystal forms, are the primary mechanism of allosteric regulation of Pfk by influencing the F6P-binding site. Whereas the nature of this conformational switch appears to be largely conserved in bacterial, yeast and mammalian Pfk, initiation of these changes differs significantly in eukaryotic Pfk.
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Crystal structure of human platelet phosphofructokinase-1 locked in an activated conformation.,Kloos M, Bruser A, Kirchberger J, Schoneberg T, Strater N Biochem J. 2015 Aug 1;469(3):421-32. doi: 10.1042/BJ20150251. Epub 2015 Jun 11. PMID:26205495<ref>PMID:26205495</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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==See Also==
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</div>
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*[[Phosphofructokinase 3D structures|Phosphofructokinase 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: 6-phosphofructokinase]]
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[[Category: Homo sapiens]]
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[[Category: Kloos, M]]
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[[Category: Large Structures]]
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[[Category: Phosphohexokinase]]
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[[Category: Kloos M]]
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[[Category: Transferase]]
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Current revision

AMPPCP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II

PDB ID 4rh3

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