3w1s

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{{STRUCTURE_3w1s| PDB=3w1s | SCENE= }}
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==Crystal structure of Saccharomyces cerevisiae Atg12-Atg5 conjugate bound to the N-terminal domain of Atg16==
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===Crystal structure of Saccharomyces cerevisiae Atg12-Atg5 conjugate bound to the N-terminal domain of Atg16===
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<StructureSection load='3w1s' size='340' side='right' caption='[[3w1s]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23238393}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3w1s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W1S FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APG5, ATG5, Atg5(amino acids 1-284), P2601, YPL149W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), APG15, APG16, ATG16, Atg16(amino acids 1-46), CVT11, SAP18, YM8520.08C, YMR159C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), APG12, ATG12, Atg12(amino acids 100-186), YBR1506, YBR217W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w1s RCSB], [http://www.ebi.ac.uk/pdbsum/3w1s PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Atg12 is conjugated to Atg5 through enzymatic reactions similar to ubiquitination. The Atg12-Atg5 conjugate functions as an E3-like enzyme to promote lipidation of Atg8, whereas lipidated Atg8 has essential roles in both autophagosome formation and selective cargo recognition during autophagy. However, the molecular role of Atg12 modification in these processes has remained elusive. Here, we report the crystal structure of the Atg12-Atg5 conjugate. In addition to the isopeptide linkage, Atg12 forms hydrophobic and hydrophilic interactions with Atg5, thereby fixing its position on Atg5. Structural comparison with unmodified Atg5 and mutational analyses showed that Atg12 modification neither induces a conformational change in Atg5 nor creates a functionally important architecture. Rather, Atg12 functions as a binding module for Atg3, the E2 enzyme for Atg8, thus endowing Atg5 with the ability to interact with Atg3 to facilitate Atg8 lipidation.
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==Function==
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Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation.,Noda NN, Fujioka Y, Hanada T, Ohsumi Y, Inagaki F EMBO Rep. 2012 Dec 14. doi: 10.1038/embor.2012.208. PMID:23238393<ref>PMID:23238393</ref>
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[[http://www.uniprot.org/uniprot/ATG5_YEAST ATG5_YEAST]] Involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Required for ATG8 association to the vesicle membranes.<ref>PMID:8921905</ref> <ref>PMID:8224160</ref> <ref>PMID:9759731</ref> <ref>PMID:10406794</ref> <ref>PMID:10712513</ref> <ref>PMID:11149920</ref> [[http://www.uniprot.org/uniprot/ATG12_YEAST ATG12_YEAST]] Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through an 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. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity.<ref>PMID:9759731</ref> <ref>PMID:8224160</ref> <ref>PMID:11149920</ref> [[http://www.uniprot.org/uniprot/ATG16_YEAST ATG16_YEAST]] Stabilizes the ATG5-ATG12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. Required for ATG8 localization to the pre-autophagosomal structure.<ref>PMID:8224160</ref> <ref>PMID:8663607</ref> <ref>PMID:10406794</ref> <ref>PMID:11689437</ref> <ref>PMID:11897782</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3w1s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1S OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:023238393</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Saccharomyces cerevisiae s288c]]
[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Fujioka, Y.]]
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[[Category: Fujioka, Y]]
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[[Category: Hanada, T.]]
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[[Category: Hanada, T]]
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[[Category: Inagaki, F.]]
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[[Category: Inagaki, F]]
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[[Category: Noda, N N.]]
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[[Category: Noda, N N]]
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[[Category: Ohsumi, Y.]]
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[[Category: Ohsumi, Y]]
[[Category: Atg3 binding]]
[[Category: Atg3 binding]]
[[Category: E3-like]]
[[Category: E3-like]]

Revision as of 07:33, 21 December 2014

Crystal structure of Saccharomyces cerevisiae Atg12-Atg5 conjugate bound to the N-terminal domain of Atg16

3w1s, resolution 2.60Å

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