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1u2x

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Revision as of 09:35, 29 September 2021

Crystal Structure of a Hypothetical ADP-dependent Phosphofructokinase from Pyrococcus horikoshii OT3

Structural highlights

1u2x is a 2 chain structure with sequence from 'pyrococcus shinkaii'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Activity:	ADP-specific phosphofructokinase, with EC number 2.7.1.146
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[K6PF_PYRHO] Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using ADP as the phosphate donor (By similarity).

Evolutionary Conservation

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

Publication Abstract from PubMed

Some hyperthermophilic archaea use a modified glycolytic pathway that employs an ADP-dependent glucokinase (ADP-GK) and an ADP-dependent phosphofructokinase (ADP-PFK) or, in the case of Methanococcus jannaschii, a bifunctional ADP-dependent glucophosphofructokinase (ADP-GK/PFK). The crystal structures of three ADP-GKs have been determined. However, there is no structural information available for ADP-PFKs or the ADP-GK/PFK. Here, we present the first crystal structure of an ADP-PFK from Pyrococcus horikoshii OT3 (PhPFK) in both apo- and AMP-bound forms determined to 2.0-A and 1.9-A resolution, respectively, along with biochemical characterization of the enzyme. The overall structure of PhPFK maintains a similar large and small alpha/beta domain structure seen in the ADP-GK structures. A large conformational change accompanies binding of phosphoryl donor, acceptor, or both, in all members of the ribokinase superfamily characterized thus far, which is believed to be critical to enzyme function. Surprisingly, no such conformational change was observed in the AMP-bound PhPFK structure compared with the apo structure. Through comprehensive site-directed mutagenesis of the substrate binding pocket we identified residues that were critical for both substrate recognition and the phosphotransfer reaction. The catalytic residues and many of the substrate binding residues are conserved between PhPFK and ADP-GKs; however, four key residues differ in the sugar-binding pocket, which we have shown determine the sugar-binding specificity. Using these results we were able to engineer a mutant PhPFK that mimics the ADP-GK/PFK and is able to phosphorylate both fructose 6-phosphate and glucose.

ADP-dependent 6-phosphofructokinase from Pyrococcus horikoshii OT3: structure determination and biochemical characterization of PH1645.,Currie MA, Merino F, Skarina T, Wong AH, Singer A, Brown G, Savchenko A, Caniuguir A, Guixe V, Yakunin AF, Jia Z J Biol Chem. 2009 Aug 21;284(34):22664-71. Epub 2009 Jun 24. PMID:19553681^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Currie MA, Merino F, Skarina T, Wong AH, Singer A, Brown G, Savchenko A, Caniuguir A, Guixe V, Yakunin AF, Jia Z. ADP-dependent 6-phosphofructokinase from Pyrococcus horikoshii OT3: structure determination and biochemical characterization of PH1645. J Biol Chem. 2009 Aug 21;284(34):22664-71. Epub 2009 Jun 24. PMID:19553681 doi:10.1074/jbc.M109.012401

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u2x"

@@ Line 3: / Line 3: @@
 <StructureSection load='1u2x' size='340' side='right'caption='[[1u2x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u2x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U2X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-specific_phosphofructokinase ADP-specific phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.146 2.7.1.146] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/ADP-specific_phosphofructokinase ADP-specific phosphofructokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.146 2.7.1.146] </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=1u2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2x OCA], [http://pdbe.org/1u2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u2x RCSB], [http://www.ebi.ac.uk/pdbsum/1u2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2x ProSAT]</span></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=1u2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2x OCA], [https://pdbe.org/1u2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2x RCSB], [https://www.ebi.ac.uk/pdbsum/1u2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/K6PF_PYRHO K6PF_PYRHO]] Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using ADP as the phosphate donor (By similarity).
+[[https://www.uniprot.org/uniprot/K6PF_PYRHO K6PF_PYRHO]] Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using ADP as the phosphate donor (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1u2x

From Proteopedia

Revision as of 09:35, 29 September 2021

Crystal Structure of a Hypothetical ADP-dependent Phosphofructokinase from Pyrococcus horikoshii OT3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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