1r4x: Difference between revisions

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-[[Image:1r4x.jpg|left|200px]]<br /><applet load="1r4x" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1r4x, resolution 1.90&Aring;" />
-'''Crystal Structure Analys of the Gamma-COPI Appendage domain'''<br />
-==Overview==
+==Crystal Structure Analys of the Gamma-COPI Appendage domain==
-COPI-coated vesicles mediate retrograde transport from the Golgi back to, the ER and intra-Golgi transport. The cytosolic precursor of the COPI, coat, the heptameric coatomer complex, can be thought of as composed of, two subcomplexes. The first consists of the beta-, gamma-, delta- and, zeta-COP subunits which are distantly homologous to AP clathrin adaptor, subunits. The second consists of the alpha-, beta'- and epsilon-COP, subunits. Here, we present the structure of the appendage domain of, gamma-COP and show that it has a similar overall fold as the, alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP, appendage possesses a single protein/protein interaction site on its, platform subdomain. We show that in yeast this site binds to the ARFGAP, Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP, appendage that interacts with the alpha,beta',epsilon COPI subcomplex.
+<StructureSection load='1r4x' size='340' side='right'caption='[[1r4x]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1r4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4X 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1r4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4x OCA], [https://pdbe.org/1r4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4x RCSB], [https://www.ebi.ac.uk/pdbsum/1r4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4x ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/COPG1_HUMAN COPG1_HUMAN] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity).<ref>PMID:20674546</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/r4/1r4x_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=1r4x ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-R4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4X OCA].
+*[[Coatomer 3D structures|Coatomer 3D structures]]
+== References ==
-==Reference==
+<references/>
-Gamma-COP appendage domain - structure and function., Watson PJ, Frigerio G, Collins BM, Duden R, Owen DJ, Traffic. 2004 Feb;5(2):79-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14690497 14690497]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Collins, B.M.]]
+[[Category: Collins BM]]
-[[Category: Duden, R.]]
+[[Category: Duden R]]
-[[Category: Frigerio, G.]]
+[[Category: Frigerio G]]
-[[Category: Owen, D.J.]]
+[[Category: Owen DJ]]
-[[Category: Watson, P.J.]]
+[[Category: Watson PJ]]
-[[Category: MG]]
-[[Category: appendage; beta sandwich; coatomer; adp-ribosylation factors]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:46:55 2008''