3tu9: Difference between revisions

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<StructureSection load='3tu9' size='340' side='right'caption='[[3tu9]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='3tu9' size='340' side='right'caption='[[3tu9]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tu9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tu9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MM:2-O-METHYL-1,6-DI-O-PHOSPHONO-D-MANNITOL'>5MM</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]] 2.09&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDOA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MM:2-O-METHYL-1,6-DI-O-PHOSPHONO-D-MANNITOL'>5MM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </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=3tu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu9 OCA], [https://pdbe.org/3tu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu9 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=3tu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu9 OCA], [https://pdbe.org/3tu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT]] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref> 
[https://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Several 5-O-alkyl- and 5-C-alkyl-mannitol bis-phosphates were synthesized and comparatively assayed as inhibitors of fructose bis-phosphate aldolases (Fbas) from rabbit muscle (taken as surrogate model of the human enzyme) and from Trypanosoma brucei. A limited selectivity was found in several instances. Crystallographic studies confirm that the 5-O-methyl derivative binds competitively with substrate and the 5-O-methyl moiety penetrating deeper into a shallow hydrophobic pocket at the active site. This observation can lead to the preparation of selective competitive or irreversible inhibitors of the parasite Fba.
 
Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases.,Mabiala-Bassiloua CG, Arthus-Cartier G, Hannaert V, Therisod H, Sygusch J, Therisod M ACS Med Chem Lett. 2011 Sep 3;2(11):804-8. doi: 10.1021/ml200129s. eCollection, 2011 Nov 10. PMID:24900268<ref>PMID:24900268</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tu9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: European rabbit]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arthus-Cartier, G]]
[[Category: Oryctolagus cuniculus]]
[[Category: Sygusch, J]]
[[Category: Arthus-Cartier G]]
[[Category: Beta-barrel]]
[[Category: Sygusch J]]
[[Category: Inhibitor docking]]
[[Category: Lyase-lyase inhibitor complex]]
[[Category: Mammalian aldolase]]
[[Category: Mannitol-bisphosphate]]
[[Category: Trypanosomal aldolase]]

Latest revision as of 16:39, 14 March 2024

Crystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphateCrystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphate

Structural highlights

3tu9 is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.09Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALDOA_RABIT Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]

See Also

References

  1. ↑ St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259 doi:10.1074/jbc.M611505200

3tu9, resolution 2.09Å

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