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[[Image:3pfk.gif|left|200px]]<br /><applet load="3pfk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3pfk, resolution 2.4&Aring;" />
'''PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL'''<br />


==Overview==
==PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL==
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.
<StructureSection load='3pfk' size='340' side='right'caption='[[3pfk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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>


==About this Structure==
==See Also==
3PFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PFK OCA].
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=6115424 6115424]
__TOC__
[[Category: 6-phosphofructokinase]]
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Evans, P R.]]
[[Category: Evans PR]]
[[Category: Hudson, P J.]]
[[Category: Hudson PJ]]
[[Category: PO4]]
[[Category: transferase(phosphotransferase)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:46 2008''

Latest revision as of 13:40, 21 February 2024

PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROLPHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL

Structural highlights

3pfk is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Byrnes M, Zhu X, Younathan ES, Chang SH. Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme. Biochemistry. 1994 Mar 22;33(11):3424-31. doi: 10.1021/bi00177a036. PMID:8136379 doi:http://dx.doi.org/10.1021/bi00177a036

3pfk, resolution 2.40Å

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