2li5
From Proteopedia
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==NMR structure of Atg8-Atg7C30 complex== | ==NMR structure of Atg8-Atg7C30 complex== | ||
| - | <StructureSection load='2li5' size='340' side='right' caption='[[2li5 | + | <StructureSection load='2li5' size='340' side='right'caption='[[2li5]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2li5]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2li5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LI5 FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <b> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2li5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li5 OCA], [https://pdbe.org/2li5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2li5 RCSB], [https://www.ebi.ac.uk/pdbsum/2li5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2li5 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATG8_YEAST ATG8_YEAST] Involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, may mediate the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Participates also in membrane fusion events that take place in the early secretory pathway.<ref>PMID:8224160</ref> <ref>PMID:7593182</ref> <ref>PMID:9649430</ref> <ref>PMID:10525546</ref> <ref>PMID:10681575</ref> <ref>PMID:10837468</ref> <ref>PMID:11038174</ref> <ref>PMID:11100732</ref> <ref>PMID:11149920</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
E1 enzymes activate ubiquitin-like proteins and transfer them to cognate E2 enzymes. Atg7, a noncanonical E1, activates two ubiquitin-like proteins, Atg8 and Atg12, and plays a crucial role in autophagy. Here, we report crystal structures of full-length Atg7 and its C-terminal domain bound to Atg8 and MgATP, as well as a solution structure of Atg8 bound to the extreme C-terminal domain (ECTD) of Atg7. The unique N-terminal domain (NTD) of Atg7 is responsible for Atg3 (E2) binding, whereas its C-terminal domain is comprised of a homodimeric adenylation domain (AD) and ECTD. The structural and biochemical data demonstrate that Atg8 is initially recognized by the C-terminal tail of ECTD and is then transferred to an AD, where the Atg8 C terminus is attacked by the catalytic cysteine to form a thioester bond. Atg8 is then transferred via a trans mechanism to the Atg3 bound to the NTD of the opposite protomer within a dimer. | E1 enzymes activate ubiquitin-like proteins and transfer them to cognate E2 enzymes. Atg7, a noncanonical E1, activates two ubiquitin-like proteins, Atg8 and Atg12, and plays a crucial role in autophagy. Here, we report crystal structures of full-length Atg7 and its C-terminal domain bound to Atg8 and MgATP, as well as a solution structure of Atg8 bound to the extreme C-terminal domain (ECTD) of Atg7. The unique N-terminal domain (NTD) of Atg7 is responsible for Atg3 (E2) binding, whereas its C-terminal domain is comprised of a homodimeric adenylation domain (AD) and ECTD. The structural and biochemical data demonstrate that Atg8 is initially recognized by the C-terminal tail of ECTD and is then transferred to an AD, where the Atg8 C terminus is attacked by the catalytic cysteine to form a thioester bond. Atg8 is then transferred via a trans mechanism to the Atg3 bound to the NTD of the opposite protomer within a dimer. | ||
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Structural basis of Atg8 activation by a homodimeric E1, Atg7.,Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F Mol Cell. 2011 Nov 4;44(3):462-75. PMID:22055191<ref>PMID:22055191</ref> | Structural basis of Atg8 activation by a homodimeric E1, Atg7.,Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F Mol Cell. 2011 Nov 4;44(3):462-75. PMID:22055191<ref>PMID:22055191</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2li5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Saccharomyces cerevisiae]] | + | [[Category: Large Structures]] |
| - | [[Category: Fujioka | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Inagaki | + | [[Category: Fujioka Y]] |
| - | [[Category: Kumeta | + | [[Category: Inagaki F]] |
| - | [[Category: Nakatogawa | + | [[Category: Kumeta H]] |
| - | [[Category: Noda | + | [[Category: Nakatogawa H]] |
| - | [[Category: Ogura | + | [[Category: Noda NN]] |
| - | [[Category: Ohsumi | + | [[Category: Ogura K]] |
| - | [[Category: Satoo | + | [[Category: Ohsumi Y]] |
| - | + | [[Category: Satoo K]] | |
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Current revision
NMR structure of Atg8-Atg7C30 complex
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