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3lge

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==Crystal structure of rabbit muscle aldolase-SNX9 LC4 complex==
==Crystal structure of rabbit muscle aldolase-SNX9 LC4 complex==
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<StructureSection load='3lge' size='340' side='right' caption='[[3lge]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='3lge' size='340' side='right'caption='[[3lge]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3lge]] is a 8 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGE FirstGlance]. <br>
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<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>
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</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 Oryctolagus cuniculus])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=3lge RCSB], [http://www.ebi.ac.uk/pdbsum/3lge PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lge_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/3lge_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lge ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3lge" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Aldolase|Aldolase]]
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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*[[Sorting nexin|Sorting nexin]]
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*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fructose-bisphosphate aldolase]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Fortin, E]]
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[[Category: Fortin E]]
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[[Category: Izard, T]]
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[[Category: Izard T]]
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[[Category: Park, H]]
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[[Category: Park H]]
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[[Category: Rangarajan, E S]]
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[[Category: Rangarajan ES]]
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[[Category: Sygusch, J]]
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[[Category: Sygusch J]]
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[[Category: Actin dynamic]]
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[[Category: Complex]]
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[[Category: Glycolysis]]
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[[Category: Hydrophobic pocket]]
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[[Category: Lc4]]
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[[Category: Lyase]]
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[[Category: Lyase-protein binding complex]]
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[[Category: Phosphoprotein]]
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[[Category: Protein transport]]
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[[Category: Schiff base]]
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[[Category: Sh3 domain]]
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[[Category: Transport]]
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Current revision

Crystal structure of rabbit muscle aldolase-SNX9 LC4 complex

PDB ID 3lge

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