3t2c: Difference between revisions

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[[Image:3t2c.png|left|200px]]


{{STRUCTURE_3t2c|  PDB=3t2c  |  SCENE=  }}
==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=''>
===Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_21983965}}
</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='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>
==About this Structure==
<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>
[[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].  
</table>
== Function ==
[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>


==See Also==
==See Also==
*[[Aldolase|Aldolase]]
*[[Aldolase 3D structures|Aldolase 3D structures]]
*[[Suggestions for new articles|Suggestions for new articles]]
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:021983965</ref><references group="xtra"/>
</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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