4xz2: Difference between revisions
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''' | ==Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I== | ||
<StructureSection load='4xz2' size='340' side='right' caption='[[4xz2]], [[Resolution|resolution]] 2.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xz2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZ2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wlo|4wlo]], [[4u1r|4u1r]], [[4rh3|4rh3]], [[4omt|4omt]], [[3opy|3opy]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xz2 RCSB], [http://www.ebi.ac.uk/pdbsum/4xz2 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. | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: 6-phosphofructokinase]] | |||
[[Category: Kloos, M]] | [[Category: Kloos, M]] | ||
[[Category: Fructose 6-phosphate]] | |||
[[Category: Human platelet phosphofructokinase]] | |||
[[Category: Main regulator of glycolysis]] | |||
[[Category: Transferase]] | |||
Revision as of 15:31, 3 June 2015
Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form IHuman platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I
Structural highlights
Function[PFKAP_HUMAN] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Publication Abstract from PubMedWhereas 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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