3mnm

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{{STRUCTURE_3mnm| PDB=3mnm | SCENE= }}
 
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===Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae===
 
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{{ABSTRACT_PUBMED_020704189}}
 
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==Function==
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==Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae==
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[[http://www.uniprot.org/uniprot/GGA2_YEAST GGA2_YEAST]] May play a role in the regulation of membrane traffic through the trans-Golgi network.<ref>PMID:10747088</ref> <ref>PMID:11124697</ref>
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<StructureSection load='3mnm' size='340' side='right'caption='[[3mnm]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3mnm]] is a 3 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=3MNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MNM FirstGlance]. <br>
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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]] 1.73&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3mnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mnm OCA], [https://pdbe.org/3mnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mnm RCSB], [https://www.ebi.ac.uk/pdbsum/3mnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mnm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GGA2_YEAST GGA2_YEAST] May play a role in the regulation of membrane traffic through the trans-Golgi network.<ref>PMID:10747088</ref> <ref>PMID:11124697</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/3mnm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=3mnm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Different assemblies of accessory proteins with clathrin are critical for transporting precisely various cargos between intracellular compartments. GGA proteins are adaptors for clathrin-mediated intracellular trafficking, connecting other accessory and cargo proteins to clathrin-coated vesicles. Both binding to the GAE domain of GGA protein yGGA2 in Saccharomyces cerevisia, Ent3 and Ent5 are involved in different trafficking pathways. Ent5 is ubiquitous and localized in a manner independent of yGGA2, and Ent3 functions preferentially through yGGA2. Not known are the sources of these differences. Here we show not all acidic-phenylalanine motifs in Ent3/5 are active for yGGA2_GAE domain binding. Two of the three acidic-phenylalanine motifs from Ent3 can bind to the yGGA2_GAE domain, while only one of the two motifs from Ent5 can bind. We also determined the crystal structure of the yGGA2_GAE domain at 1.8 A resolution. Structural docking and mutagenesis analysis shows inactive motifs in Ent3 and Ent5 repel yGGA2_GAE binding through disfavored residues at positions 1 and 3. These results suggest accessory proteins may fine-tune the GGA adaptor dependence by adjusting their non-acidic-phenylalanine residues, thus contributing to the distinct role of Ent3 and Ent5 in trafficking.
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==About this Structure==
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Structural basis for the specificity of the GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5 .,Fang P, Li X, Wang J, Niu L, Teng M Biochemistry. 2010 Sep 14;49(36):7949-55. PMID:20704189<ref>PMID:20704189</ref>
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[[3mnm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MNM OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 3mnm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Fang, P.]]
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[[Category: Fang P]]
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[[Category: Li, X.]]
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[[Category: Li X]]
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[[Category: Niu, L.]]
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[[Category: Niu L]]
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[[Category: Teng, M.]]
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[[Category: Teng M]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: Beta sandwich]]
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[[Category: Ig-like]]
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[[Category: Protein transport]]
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Current revision

Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae

PDB ID 3mnm

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