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. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMT OCA]. <br> | <table><tr><td colspan='2'>[[4omt]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OMT FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8n|3o8n]], [[3opy|3opy]]</td></tr> | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8n|3o8n]], [[3opy|3opy]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [http://www.ebi.ac.uk/pdbsum/4omt PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [http://www.ebi.ac.uk/pdbsum/4omt PDBsum]</span></td></tr> | ||
<table> | <table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/K6PF_HUMAN K6PF_HUMAN]] Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.[HAMAP-Rule:MF_00339] | [[http://www.uniprot.org/uniprot/K6PF_HUMAN K6PF_HUMAN]] Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.[HAMAP-Rule:MF_00339] | ||
<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 == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:53, 24 September 2014
Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysisCrystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis
Structural highlights
Disease[K6PF_HUMAN] Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by mutations affecting the gene represented in this entry. Function[K6PF_HUMAN] Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.[HAMAP-Rule:MF_00339] 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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