2dyt

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[[Image:2dyt.gif|left|200px]]
 
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==The crystal structure of Saccharomyces cerevisiae Atg3==
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The line below this paragraph, containing "STRUCTURE_2dyt", creates the "Structure Box" on the page.
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<StructureSection load='2dyt' size='340' side='right'caption='[[2dyt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2dyt]] 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=2DYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DYT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2dyt| PDB=2dyt | SCENE= }}
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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=2dyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyt OCA], [https://pdbe.org/2dyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dyt RCSB], [https://www.ebi.ac.uk/pdbsum/2dyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dyt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATG3_YEAST ATG3_YEAST] E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt).<ref>PMID:9023185</ref> <ref>PMID:8224160</ref> <ref>PMID:8050581</ref> <ref>PMID:11100732</ref> <ref>PMID:11149920</ref> <ref>PMID:15277523</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/dy/2dyt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2dyt ConSurf].
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<div style="clear:both"></div>
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'''The crystal structure of Saccharomyces cerevisiae Atg3'''
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==See Also==
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*[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]]
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== References ==
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==Overview==
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<references/>
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Atg3 is an E2-like enzyme that catalyzes the conjugation of Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, which is the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. We report here the crystal structure of Saccharomyces cerevisiae Atg3 at 2.5-A resolution. Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region, one of which consists of approximately 80 residues and has a random coil structure in solution and another with a long alpha-helical structure that protrudes from the core region as far as 30 A. In vivo and in vitro analyses suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding Atg8. A sulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE. The structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg3 carries out.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2DYT is a [[Single protein]] structure of 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=2DYT OCA].
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==Reference==
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The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation., Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 16;282(11):8036-43. Epub 2007 Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17227760 17227760]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Inagaki F]]
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[[Category: Inagaki, F.]]
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[[Category: Suzuki NN]]
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[[Category: Suzuki, N N.]]
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[[Category: Yamada Y]]
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[[Category: Yamada, Y.]]
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[[Category: E2 fold]]
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[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:38:08 2008''
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Current revision

The crystal structure of Saccharomyces cerevisiae Atg3

PDB ID 2dyt

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