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| | ==Structure of Toxoplasma gondii fructose 1,6 bisphosphate aldolase== | | ==Structure of Toxoplasma gondii fructose 1,6 bisphosphate aldolase== |
| - | <StructureSection load='4tu1' size='340' side='right' caption='[[4tu1]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4tu1' size='340' side='right'caption='[[4tu1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tu1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TU1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tu1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TU1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGVEG_236040 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://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=4tu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu1 OCA], [https://pdbe.org/4tu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tu1 RCSB], [https://www.ebi.ac.uk/pdbsum/4tu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu1 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=4tu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu1 OCA], [http://pdbe.org/4tu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tu1 RCSB], [http://www.ebi.ac.uk/pdbsum/4tu1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B9PW35_TOXGV B9PW35_TOXGV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4tu1" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4tu1" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fructose-bisphosphate aldolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Toxgo]] | + | [[Category: Toxoplasma gondii]] |
| - | [[Category: Bosch, J]] | + | [[Category: Bosch J]] |
| - | [[Category: Boucher, L E]] | + | [[Category: Boucher LE]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: F16bp]]
| + | |
| - | [[Category: Glideosome]]
| + | |
| - | [[Category: Invasion]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Toxoplasma]]
| + | |
| Structural highlights
Function
B9PW35_TOXGV
Publication Abstract from PubMed
The apicomplexan parasite Toxoplasma gondii must invade host cells to continue its lifecycle. It invades different cell types using an actomyosin motor that is connected to extracellular adhesins via the bridging protein fructose-1,6-bisphosphate aldolase. During invasion, aldolase serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway. Crystal structures of the homologous Plasmodium falciparum fructose-1,6-bisphosphate aldolase have been described previously. Here, T. gondii fructose-1,6-bisphosphate aldolase has been crystallized in space group P22121, with the biologically relevant tetramer in the asymmetric unit, and the structure has been determined via molecular replacement to a resolution of 2.0 A. An analysis of the quality of the model and of the differences between the four chains in the asymmetric unit and a comparison between the T. gondii and P. falciparum aldolase structures is presented.
Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase.,Boucher LE, Bosch J Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1186-92. doi:, 10.1107/S2053230X14017087. Epub 2014 Aug 29. PMID:25195889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boucher LE, Bosch J. Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1186-92. doi:, 10.1107/S2053230X14017087. Epub 2014 Aug 29. PMID:25195889 doi:http://dx.doi.org/10.1107/S2053230X14017087
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