4wl0: Difference between revisions

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 ==Ligand-free structure of human platelet phosphofructokinase in an R-state, crystal form I==
-<StructureSection load='4wl0' size='340' side='right' caption='[[4wl0]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
+<StructureSection load='4wl0' size='340' side='right'caption='[[4wl0]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wl0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WL0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wl0]] 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=4WL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WL0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.89&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1r|4u1r]], [[4rh3|4rh3]], [[4omt|4omt]], [[3opy|3opy]], [[4xz2|4xz2]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wl0 OCA], [https://pdbe.org/4wl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wl0 RCSB], [https://www.ebi.ac.uk/pdbsum/4wl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wl0 ProSAT]</span></td></tr>
-<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=4wl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wl0 RCSB], [http://www.ebi.ac.uk/pdbsum/4wl0 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[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.
+[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.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Whereas the three-dimensional structure and the structural basis of the allosteric regulation of prokaryotic 6-phosphofructokinases (Pfks) have been studied in great detail, knowledge of the molecular basis of the allosteric behaviour of the far more complex mammalian Pfks is still very limited. The human muscle isozyme was expressed heterologously in yeast cells and purified using a five-step purification protocol. Protein crystals suitable for diffraction experiments were obtained by the vapour-diffusion method. The crystals belonged to space group P6222 and diffracted to 6.0 A resolution. The 3.2 A resolution structure of rabbit muscle Pfk (rmPfk) was placed into the asymmetric unit and optimized by rigid-body and group B-factor refinement. Interestingly, the tetrameric enzyme dissociated into a dimer, similar to the situation observed in the structure of rmPfk.
-Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis.,Kloos M, Bruser A, Kirchberger J, Schoneberg T, Strater N Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):578-82. doi:, 10.1107/S2053230X14008723. Epub 2014 Apr 25. PMID:24817713<ref>PMID:24817713</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: 6-phosphofructokinase]]
+[[Category: Homo sapiens]]
-[[Category: Kloos, M]]
+[[Category: Large Structures]]
-[[Category: Fructose 6-phosphate]]
+[[Category: Kloos M]]
-[[Category: Human platelet phosphofructokinase]]
+[[Category: Strater N]]
-[[Category: Main regulator of glycolysis]]
-[[Category: Transferase]]