2f48
From Proteopedia
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| - | [[Image:2f48.png|left|200px]] | ||
| - | + | ==Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi== | |
| - | + | <StructureSection load='2f48' size='340' side='right'caption='[[2f48]], [[Resolution|resolution]] 2.11Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2f48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F48 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</td></tr> | |
| - | == | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene></td></tr> |
| - | [[2f48]] is a 2 chain structure with sequence from [ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f48 OCA], [https://pdbe.org/2f48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f48 RCSB], [https://www.ebi.ac.uk/pdbsum/2f48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f48 ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/PFP_BORBU PFP_BORBU] Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01980]<ref>PMID:10545221</ref> |
| - | [[Category: | + | == Evolutionary Conservation == |
| - | [[Category: | + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/2f48_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f48 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Borreliella burgdorferi B31]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wang M]] | ||
Current revision
Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi
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