View source for 5xoe


==Crystal Structure of the apo Staphylococcus aureus phosphofructokinase==
<StructureSection load='5xoe' size='340' side='right'caption='[[5xoe]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xoe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XOE 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]] 2.98&#8491;</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=5xoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xoe OCA], [https://pdbe.org/5xoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xoe RCSB], [https://www.ebi.ac.uk/pdbsum/5xoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xoe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PFKA_STAAB PFKA_STAAB] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
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== Publication Abstract from PubMed ==
Most reported bacterial phosphofructokinases (Pfks) are tetramers that exhibit activity allosterically regulated via conformational changes between the R and T states. We report that the Pfk from Staphylococcus aureus NCTC 8325 ( SaPfk) exists as both an active tetramer and an inactive dimer in solution. Multiple effectors, including pH, ADP, ATP, and adenylyl-imidodiphosphate (AMP-PNP), cause equilibrium shifts from the tetramer to dimer, whereas the substrate F6P stabilizes SaPfk tetrameric assembly. Crystal structures of SaPfk in complex with different ligands and biochemical analysis reveal that the flexibility of the Gly150-Leu151 motif in helix alpha7 plays a role in tetramer-dimer conversion. Thus, we propose a molecular mechanism for allosteric regulation of bacterial Pfk via conversion between the tetramer and dimer in addition to the well-characterized R-state/T-state mechanism.

Structural Insights into the Regulation of Staphylococcus aureus Phosphofructokinase by Tetramer-Dimer Conversion.,Tian T, Wang C, Wu M, Zhang X, Zang J Biochemistry. 2018 Jul 24;57(29):4252-4262. doi: 10.1021/acs.biochem.8b00028., Epub 2018 Jul 9. PMID:29940104<ref>PMID:29940104</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
[[Category: Tian T]]
[[Category: Wang C]]
[[Category: Zang J]]