1wz3: Difference between revisions

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@@ Line 3: / Line 3: @@
 <StructureSection load='1wz3' size='340' side='right'caption='[[1wz3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ3 FirstGlance]. <br>
-</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=1wz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz3 OCA], [https://pdbe.org/1wz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz3 ProSAT]</span></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]] 1.8&#8491;</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=1wz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz3 OCA], [https://pdbe.org/1wz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/AT12B_ARATH AT12B_ARATH]] Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. ATG12/ATG5 conjugate has an essential role in plant nutrient recycling.
+[https://www.uniprot.org/uniprot/AT12B_ARATH AT12B_ARATH] Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. ATG12/ATG5 conjugate has an essential role in plant nutrient recycling.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 19: @@
 </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=1wz3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Atg12 is a post-translational modifier that is activated and conjugated to its single target, Atg5, by a ubiquitin-like conjugation system. The Atg12-Atg5 conjugate is essential for autophagy, the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. Here, we demonstrate that the Atg12 conjugation system exists in Arabidopsis and is essential for plant autophagy as well as in yeast and mammals. We also report the crystal structure of Arabidopsis thaliana (At) ATG12 at 1.8 A resolution. Despite no obvious sequence homology with ubiquitin, the structure of AtATG12 shows a ubiquitin fold strikingly similar to those of mammalian homologs of Atg8, the other ubiquitin-like modifier essential for autophagy, which is conjugated to phosphatidylethanolamine. Two types of hydrophobic patches are present on the surface of AtATG12: one is conserved in both Atg12 and Atg8 orthologs, while the other is unique to Atg12 orthologs. Considering that they share Atg7 as an E1-like enzyme, we suggest that the first hydrophobic patch is responsible for the conjugation reaction, while the latter is involved in Atg12-specific functions.
-The crystal structure of plant ATG12 and its biological implication in autophagy.,Suzuki NN, Yoshimoto K, Fujioka Y, Ohsumi Y, Inagaki F Autophagy. 2005 Jul;1(2):119-26. Epub 2005 Jul 23. PMID:16874047<ref>PMID:16874047</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1wz3" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Fujioka, Y]]
+[[Category: Fujioka Y]]
-[[Category: Inagaki, F]]
+[[Category: Inagaki F]]
-[[Category: Ohsumi, Y]]
+[[Category: Ohsumi Y]]
-[[Category: Suzuki, N N]]
+[[Category: Suzuki NN]]
-[[Category: Yoshimoto, K]]
+[[Category: Yoshimoto K]]
-[[Category: Plant protein]]
-[[Category: Ubiquitin-fold]]

1wz3: Difference between revisions

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