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3g9h
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3g9h is ON HOLD Authors: Reider, A., Barker, S., Mishra, S., Im, Y.J., Maldonado-Baez, L., Hurley, J., Traub, L., Wendland, B. Description: Crystal...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the C-terminal mu homology domain of Syp1== | |
| - | + | <StructureSection load='3g9h' size='340' side='right'caption='[[3g9h]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3g9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9H FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene></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=3g9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9h OCA], [https://pdbe.org/3g9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9h RCSB], [https://www.ebi.ac.uk/pdbsum/3g9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9h ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SYP1_YEAST SYP1_YEAST] Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.<ref>PMID:11014808</ref> <ref>PMID:18791237</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/3g9h_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3g9h ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Barker S]] | ||
| + | [[Category: Hurley J]] | ||
| + | [[Category: Im YJ]] | ||
| + | [[Category: Maldonado-Baez L]] | ||
| + | [[Category: Mishra S]] | ||
| + | [[Category: Reider A]] | ||
| + | [[Category: Traub L]] | ||
| + | [[Category: Wendland B]] | ||
Current revision
Crystal structure of the C-terminal mu homology domain of Syp1
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