3t2c: Difference between revisions

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==Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form==
==Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form==
<StructureSection load='3t2c' size='340' side='right' caption='[[3t2c]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='3t2c' size='340' side='right'caption='[[3t2c]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3t2c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoproteus_neutrophilus Thermoproteus neutrophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T2C FirstGlance]. <br>
<table><tr><td colspan='2'>[[3t2c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_neutrophilum_V24Sta Pyrobaculum neutrophilum V24Sta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T2C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t2b|3t2b]], [[3t2d|3t2d]], [[3t2e|3t2e]], [[3t2f|3t2f]], [[3t2g|3t2g]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tneu_0133 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70771 Thermoproteus neutrophilus])</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=3t2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t2c OCA], [https://pdbe.org/3t2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t2c RCSB], [https://www.ebi.ac.uk/pdbsum/3t2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t2c ProSAT]</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=3t2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t2c RCSB], [http://www.ebi.ac.uk/pdbsum/3t2c PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/FBPAP_PYRNV FBPAP_PYRNV] Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).<ref>PMID:20348906</ref> <ref>PMID:21983965</ref>  
Fructose-1,6-bisphosphate (FBP) aldolase/phosphatase is a bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages. It mediates the aldol condensation of heat-labile dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP) to FBP, as well as the subsequent, irreversible hydrolysis of the product to yield the stable fructose-6-phosphate (F6P) and inorganic phosphate; no reaction intermediates are released. Here we present a series of structural snapshots of the reaction that reveal a substantial remodelling of the active site through the movement of loop regions that create different catalytic functionalities at the same location. We have solved the three-dimensional structures of FBP aldolase/phosphatase from thermophilic Thermoproteus neutrophilus in a ligand-free state as well as in complex with the substrates DHAP and FBP and the product F6P to resolutions up to 1.3 A. In conjunction with mutagenesis data, this pinpoints the residues required for the two reaction steps and shows that the sequential binding of additional Mg(2+) cations reversibly facilitates the reaction. FBP aldolase/phosphatase is an ancestral gluconeogenic enzyme optimized for high ambient temperatures, and our work resolves how consecutive structural rearrangements reorganize the catalytic centre of the protein to carry out two canonical reactions in a very non-canonical type of bifunctionality.
 
Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.,Du J, Say RF, Lu W, Fuchs G, Einsle O Nature. 2011 Oct 9. doi: 10.1038/nature10458. PMID:21983965<ref>PMID:21983965</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Aldolase|Aldolase]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
*[[Suggestions for new articles|Suggestions for new articles]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thermoproteus neutrophilus]]
[[Category: Large Structures]]
[[Category: Du, J]]
[[Category: Pyrobaculum neutrophilum V24Sta]]
[[Category: Einsle, O]]
[[Category: Du J]]
[[Category: Fuchs, G]]
[[Category: Einsle O]]
[[Category: Lue, W]]
[[Category: Fuchs G]]
[[Category: Say, R]]
[[Category: Lue W]]
[[Category: Dhap]]
[[Category: Say R]]
[[Category: F6p]]
[[Category: Fbp]]
[[Category: Gap]]
[[Category: Hydrolase]]
[[Category: Lyase]]
[[Category: Phosphorylation]]

Latest revision as of 16:15, 14 March 2024

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound formFructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form

Structural highlights

3t2c is a 1 chain structure with sequence from Pyrobaculum neutrophilum V24Sta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FBPAP_PYRNV Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).[1] [2]

See Also

References

  1. ↑ Say RF, Fuchs G. Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme. Nature. 2010 Apr 15;464(7291):1077-81. PMID:20348906 doi:10.1038/nature08884
  2. ↑ Du J, Say RF, Lu W, Fuchs G, Einsle O. Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase. Nature. 2011 Oct 9. doi: 10.1038/nature10458. PMID:21983965 doi:10.1038/nature10458

3t2c, resolution 1.30Å

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