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[[Image:2dym.jpg|left|200px]]<br /><applet load="2dym" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2dym, resolution 2.20&Aring;" />
'''The crystal structure of Saccharomyces cerevisiae Atg5- Atg16(1-46) complex'''<br />


==Overview==
==The crystal structure of Saccharomyces cerevisiae Atg5- Atg16(1-46) complex==
Atg5 is covalently modified with a ubiquitin-like modifier, Atg12, and the, Atg12-Atg5 conjugate further forms a complex with the multimeric protein, Atg16. The Atg12-Atg5.Atg16 multimeric complex plays an essential role in, autophagy, the bulk degradation system conserved in all eukaryotes. We, have reported here the crystal structure of Atg5 complexed with the, N-terminal region of Atg16 at 1.97A resolution. Atg5 comprises two, ubiquitin-like domains that flank a helix-rich domain. The N-terminal, region of Atg16 has a helical structure and is bound to the groove formed, by these three domains. In vitro analysis showed that Arg-35 and Phe-46 of, Atg16 are crucial for the interaction. Atg16, with a mutation at these, residues, failed to localize to the pre-autophagosomal structure and could, not restore autophagy in Atg16-deficient yeast strains. Furthermore, these, Atg16 mutants could not restore a severe reduction in the formation of the, Atg8-phosphatidylethanolamine conjugate, another essential factor for, autophagy, in Atg16-deficient strains under starvation conditions. These, results taken together suggest that the direct interaction between Atg5, and Atg16 is crucial to the performance of their roles in autophagy.
<StructureSection load='2dym' size='340' side='right'caption='[[2dym]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dym]] is a 8 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=2DYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DYM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=2dym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dym OCA], [https://pdbe.org/2dym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dym RCSB], [https://www.ebi.ac.uk/pdbsum/2dym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dym ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/2dym_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2dym ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2DYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2DYM OCA].
*[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]]
 
== References ==
==Reference==
<references/>
Structure of Atg5.Atg16, a complex essential for autophagy., Matsushita M, Suzuki NN, Obara K, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 2;282(9):6763-72. Epub 2006 Dec 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17192262 17192262]
__TOC__
[[Category: Protein complex]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Inagaki, F.]]
[[Category: Inagaki F]]
[[Category: Matsushita, M.]]
[[Category: Matsushita M]]
[[Category: Suzuki, N.N.]]
[[Category: Suzuki NN]]
[[Category: herix-bundle]]
[[Category: ubiquitin-fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:37:23 2008''

Latest revision as of 16:48, 13 March 2024

The crystal structure of Saccharomyces cerevisiae Atg5- Atg16(1-46) complexThe crystal structure of Saccharomyces cerevisiae Atg5- Atg16(1-46) complex

Structural highlights

2dym is a 8 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATG5_YEAST Involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Required for ATG8 association to the vesicle membranes.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

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

See Also

References

  1. Kametaka S, Matsuura A, Wada Y, Ohsumi Y. Structural and functional analyses of APG5, a gene involved in autophagy in yeast. Gene. 1996 Oct 31;178(1-2):139-43. PMID:8921905
  2. Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 1993 Oct 25;333(1-2):169-74. PMID:8224160
  3. Mizushima N, Noda T, Yoshimori T, Tanaka Y, Ishii T, George MD, Klionsky DJ, Ohsumi M, Ohsumi Y. A protein conjugation system essential for autophagy. Nature. 1998 Sep 24;395(6700):395-8. PMID:9759731 doi:10.1038/26506
  4. Mizushima N, Noda T, Ohsumi Y. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J. 1999 Jul 15;18(14):3888-96. PMID:10406794 doi:10.1093/emboj/18.14.3888
  5. George MD, Baba M, Scott SV, Mizushima N, Garrison BS, Ohsumi Y, Klionsky DJ. Apg5p functions in the sequestration step in the cytoplasm-to-vacuole targeting and macroautophagy pathways. Mol Biol Cell. 2000 Mar;11(3):969-82. PMID:10712513
  6. Kim J, Huang WP, Klionsky DJ. Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex. J Cell Biol. 2001 Jan 8;152(1):51-64. PMID:11149920

2dym, resolution 2.20Å

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