4v4l
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v4l]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vt4 1vt4] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3iz8 3iz8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4L FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v4l]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vt4 1vt4] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3iz8 3iz8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4L FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4l OCA], [https://pdbe.org/4v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4l RCSB], [https://www.ebi.ac.uk/pdbsum/4v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4l 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=4v4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4l OCA], [https://pdbe.org/4v4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4l RCSB], [https://www.ebi.ac.uk/pdbsum/4v4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q7KLI1_DROME Q7KLI1_DROME] | [https://www.uniprot.org/uniprot/Q7KLI1_DROME Q7KLI1_DROME] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The Drosophila Apaf-1 related killer forms an apoptosome in the intrinsic cell death pathway. In this study we show that Dark forms a single ring when initiator procaspases are bound. This Dark-Dronc complex cleaves DrICE efficiently; hence, a single ring represents the Drosophila apoptosome. We then determined the 3D structure of a double ring at approximately 6.9 A resolution and created a model of the apoptosome. Subunit interactions in the Dark complex are similar to those in Apaf-1 and CED-4 apoptosomes, but there are significant differences. In particular, Dark has "lost" a loop in the nucleotide-binding pocket, which opens a path for possible dATP exchange in the apoptosome. In addition, caspase recruitment domains (CARDs) form a crown on the central hub of the Dark apoptosome. This CARD geometry suggests that conformational changes will be required to form active Dark-Dronc complexes. When taken together, these data provide insights into apoptosome structure, function, and evolution. | ||
| - | |||
| - | Structure of the Drosophila apoptosome at 6.9 a resolution.,Yuan S, Yu X, Topf M, Dorstyn L, Kumar S, Ludtke SJ, Akey CW Structure. 2011 Jan 12;19(1):128-40. PMID:21220123<ref>PMID:21220123</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4v4l" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cell death protein 3D structures|Cell death protein 3D structures]] | *[[Cell death protein 3D structures|Cell death protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Current revision
Structure of the Drosophila apoptosome
| |||||||||
