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1wz3

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Revision as of 06:30, 6 October 2021

The crystal structure of plant ATG12

Structural highlights

1wz3 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Suzuki NN, Yoshimoto K, Fujioka Y, Ohsumi Y, Inagaki F. The crystal structure of plant ATG12 and its biological implication in autophagy. Autophagy. 2005 Jul;1(2):119-26. Epub 2005 Jul 23. PMID:16874047

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wz3"

@@ 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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><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=1wz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz3 OCA], [http://pdbe.org/1wz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1wz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz3 ProSAT]</span></td></tr>
+</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 ==
-[[http://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]]

1wz3

From Proteopedia

Revision as of 06:30, 6 October 2021

The crystal structure of plant ATG12

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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