4omt: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of human muscle phosphofructokinase (dissociated homodimer)== | ==Crystal structure of human muscle phosphofructokinase (dissociated homodimer)== | ||
<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=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8n|3o8n]], [[3opy|3opy]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8n|3o8n]], [[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='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=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 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=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [http://pdbe.org/4omt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [http://www.ebi.ac.uk/pdbsum/4omt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4omt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| Line 19: | Line 20: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4omt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphofructokinase (PFK)|Phosphofructokinase (PFK)]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:00, 2 January 2017
Crystal structure of human muscle phosphofructokinase (dissociated homodimer)Crystal structure of human muscle phosphofructokinase (dissociated homodimer)
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. See AlsoReferences
|
| ||||||||||||||||||