4wzg
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wzg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZG FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wzg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZG FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></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=4wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzg OCA], [https://pdbe.org/4wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzg RCSB], [https://www.ebi.ac.uk/pdbsum/4wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzg ProSAT]</span></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=4wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzg OCA], [https://pdbe.org/4wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzg RCSB], [https://www.ebi.ac.uk/pdbsum/4wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ATGA1_HUMAN ATGA1_HUMAN] Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation.<ref>PMID:19287211</ref> <ref>PMID:19597335</ref> | [https://www.uniprot.org/uniprot/ATGA1_HUMAN ATGA1_HUMAN] Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation.<ref>PMID:19287211</ref> <ref>PMID:19597335</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ATG101 is an essential component of the ULK complex responsible for initiating cellular autophagy in mammalian cells; its 3-dimensional structure and molecular function, however, are currently unclear. Here we present the X-ray structure of human ATG101. The protein displays an open HORMA domain fold. Both structural properties and biophysical evidence indicate that ATG101 is locked in this conformation, in contrast to the prototypical HORMA domain protein MAD2. Moreover, we discuss a potential mode of dimerization with ATG13 as a fundamental aspect of ATG101 function. | ||
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| - | The mammalian autophagy initiator complex contains two HORMA domain proteins.,Michel M, Schwarten M, Decker C, Nagel-Steger L, Willbold D, Weiergraber OH Autophagy. 2015 Aug 3:0. PMID:26236954<ref>PMID:26236954</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4wzg" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Structure of human ATG101
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