4omt: Difference between revisions
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<StructureSection load='4omt' size='340' side='right'caption='[[4omt]], [[Resolution|resolution]] 6.00Å' scene=''> | <StructureSection load='4omt' size='340' side='right'caption='[[4omt]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4omt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4omt]] 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=4OMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6Å</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=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [https://pdbe.org/4omt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [https://www.ebi.ac.uk/pdbsum/4omt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omt ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/PFKAM_HUMAN PFKAM_HUMAN] Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PFKAM_HUMAN PFKAM_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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Phosphofructokinase | *[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kloos | [[Category: Kloos M]] | ||
[[Category: Straeter | [[Category: Straeter N]] | ||
Latest revision as of 20:16, 20 September 2023
Crystal structure of human muscle phosphofructokinase (dissociated homodimer)Crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structural highlights
DiseasePFKAM_HUMAN Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by variants affecting the gene represented in this entry. FunctionPFKAM_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. See AlsoReferences
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