3pfk: Difference between revisions

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-[[Image:3pfk.gif|left|200px]]
- {{Structure
+==PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL==
-|PDB= 3pfk |SIZE=350|CAPTION= <scene name='initialview01'>3pfk</scene>, resolution 2.4&Aring;
+<StructureSection load='3pfk' size='340' side='right'caption='[[3pfk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
+<table><tr><td colspan='2'>[[3pfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PFK FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfk OCA], [https://pdbe.org/3pfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pfk RCSB], [https://www.ebi.ac.uk/pdbsum/3pfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pfk ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfk OCA], [http://www.ebi.ac.uk/pdbsum/3pfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3pfk RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/PFKA_GEOSE PFKA_GEOSE] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]<ref>PMID:8136379</ref>
+== Evolutionary Conservation ==
+[[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/pf/3pfk_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=3pfk ConSurf].
+<div style="clear:both"></div>
-'''PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL'''
+==See Also==
+*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
+== References ==
-==Overview==
+<references/>
-Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The crystal structure of the active conformation of the enzyme has been solved to 2.4 A resolution, and three ligand-binding sites have been located. Two of these form the active site and bind the substrates F6P and ATP. The third site binds both allosteric activator and inhibitor. The complex of the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the refined model of ADP and a 6 A resolution map of bound 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl transfer. The binding of the phosphate of F6P involves two arginines from a neighbouring subunit in the tetramer, which suggests that a rearrangement of the subunits could explain the cooperativity of substrate binding. The activatory ADP is also bound by residues from two subunits.
+__TOC__
+</StructureSection>
-==About this Structure==
-PFK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA].
-==Reference==
-Phosphofructokinase: structure and control., Evans PR, Farrants GW, Hudson PJ, Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):53-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6115424 6115424]
-[[Category: 6-phosphofructokinase]]
 [[Category: Geobacillus stearothermophilus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Evans, P R.]]
+[[Category: Evans PR]]
-[[Category: Hudson, P J.]]
+[[Category: Hudson PJ]]
-[[Category: transferase(phosphotransferase)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:35:20 2008''