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| | <StructureSection load='3lge' size='340' side='right'caption='[[3lge]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3lge' size='340' side='right'caption='[[3lge]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lge]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lge]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LGE FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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]] 2.2Å</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=3lge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lge OCA], [https://pdbe.org/3lge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lge RCSB], [https://www.ebi.ac.uk/pdbsum/3lge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lge 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=3lge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lge OCA], [http://pdbe.org/3lge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lge RCSB], [http://www.ebi.ac.uk/pdbsum/3lge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lge ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/SNX9_HUMAN SNX9_HUMAN]] May be involved in several stages of intracellular trafficking. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate.<ref>PMID:11799118</ref> <ref>PMID:12952949</ref> <ref>PMID:15703209</ref> <ref>PMID:17609109</ref> <ref>PMID:18388313</ref> <ref>PMID:20427313</ref> <ref>PMID:21048941</ref> <ref>PMID:17948057</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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Aldolase 3D structures|Aldolase 3D structures]] | | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| - | *[[Sorting nexin|Sorting nexin]] | + | *[[Sorting nexin 3D structures|Sorting nexin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: European rabbit]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Fructose-bisphosphate aldolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fortin, E]] | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Izard, T]] | + | [[Category: Fortin E]] |
| - | [[Category: Park, H]] | + | [[Category: Izard T]] |
| - | [[Category: Rangarajan, E S]] | + | [[Category: Park H]] |
| - | [[Category: Sygusch, J]] | + | [[Category: Rangarajan ES]] |
| - | [[Category: Acetylation]]
| + | [[Category: Sygusch J]] |
| - | [[Category: Actin dynamic]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Hydrophobic pocket]]
| + | |
| - | [[Category: Lc4]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Lyase-protein binding complex]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Schiff base]]
| + | |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
ALDOA_RABIT Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]
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
Sorting nexin 9 (SNX9) functions in a complex with the GTPase dynamin-2 at clathrin-coated pits, where it provokes fission of vesicles to complete endocytosis. Here the SNX9.dynamin-2 complex binds to clathrin and adapter protein complex 2 (AP-2) that line these pits, and this occurs through interactions of the low complexity domain (LC4) of SNX9 with AP-2. Intriguingly, localization of the SNX9.dynamin-2 complex to clathrin-coated pits is blocked by interactions with the abundant glycolytic enzyme aldolase, which also binds to the LC4 domain of SNX9. The crystal structure of the LC4 motif of human SNX9 in complex with aldolase explains the biochemistry and biology of this interaction, where SNX9 binds near the active site of aldolase via residues 165-171 that are also required for the interactions of SNX9 with AP-2. Accordingly, SNX9 binding to aldolase is structurally precluded by the binding of substrate to the active site. Interactions of SNX9 with aldolase are far more extensive and differ from those of the actin-nucleating factor WASP with aldolase, indicating considerable plasticity in mechanisms that direct the functions of the aldolase as a scaffold protein.
Mechanism of aldolase control of sorting nexin 9 function in endocytosis.,Rangarajan ES, Park H, Fortin E, Sygusch J, Izard T J Biol Chem. 2010 Apr 16;285(16):11983-90. Epub 2010 Feb 2. PMID:20129922[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Rangarajan ES, Park H, Fortin E, Sygusch J, Izard T. Mechanism of aldolase control of sorting nexin 9 function in endocytosis. J Biol Chem. 2010 Apr 16;285(16):11983-90. Epub 2010 Feb 2. PMID:20129922 doi:10.1074/jbc.M109.092049
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