7mp9: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 phosphorylated at Ser205 in complex with ADP analog== | ==Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 phosphorylated at Ser205 in complex with ADP analog== | ||
<StructureSection load='7mp9' size='340' side='right'caption='[[7mp9]]' scene=''> | <StructureSection load='7mp9' size='340' side='right'caption='[[7mp9]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MP9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7mp9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MP9 FirstGlance]. <br> | ||
</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=7mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mp9 OCA], [https://pdbe.org/7mp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mp9 RCSB], [https://www.ebi.ac.uk/pdbsum/7mp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mp9 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AN2:AMP+PHOSPHORAMIDATE'>AN2</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=7mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mp9 OCA], [https://pdbe.org/7mp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mp9 RCSB], [https://www.ebi.ac.uk/pdbsum/7mp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mp9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mutations in PINK1 cause autosomal-recessive Parkinson's disease. Mitochondrial damage results in PINK1 import arrest on the translocase of the outer mitochondrial membrane (TOM) complex, resulting in the activation of its ubiquitin kinase activity by autophosphorylation and initiation of Parkin-dependent mitochondrial clearance. Herein, we report crystal structures of the entire cytosolic domain of insect PINK1. Our structures reveal a dimeric autophosphorylation complex targeting phosphorylation at the invariant Ser205 (human Ser228). The dimer interface requires insert 2, which is unique to PINK1. The structures also reveal how an N-terminal helix binds to the C-terminal extension and provide insights into stabilization of PINK1 on the core TOM complex. | |||
Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex.,Rasool S, Veyron S, Soya N, Eldeeb MA, Lukacs GL, Fon EA, Trempe JF Mol Cell. 2021 Nov 26. pii: S1097-2765(21)00991-6. doi:, 10.1016/j.molcel.2021.11.012. PMID:34875213<ref>PMID:34875213</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7mp9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rasool S]] | [[Category: Rasool, S]] | ||
[[Category: Trempe | [[Category: Trempe, J F]] | ||
[[Category: Veyron S]] | [[Category: Veyron, S]] | ||
[[Category: Kinase]] | |||
[[Category: Signaling protein]] | |||
[[Category: Transphorylation]] | |||
Revision as of 18:37, 22 December 2021
Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 phosphorylated at Ser205 in complex with ADP analogCrystal structure of the cytosolic domain of Tribolium castaneum PINK1 phosphorylated at Ser205 in complex with ADP analog
Structural highlights
Publication Abstract from PubMedMutations in PINK1 cause autosomal-recessive Parkinson's disease. Mitochondrial damage results in PINK1 import arrest on the translocase of the outer mitochondrial membrane (TOM) complex, resulting in the activation of its ubiquitin kinase activity by autophosphorylation and initiation of Parkin-dependent mitochondrial clearance. Herein, we report crystal structures of the entire cytosolic domain of insect PINK1. Our structures reveal a dimeric autophosphorylation complex targeting phosphorylation at the invariant Ser205 (human Ser228). The dimer interface requires insert 2, which is unique to PINK1. The structures also reveal how an N-terminal helix binds to the C-terminal extension and provide insights into stabilization of PINK1 on the core TOM complex. Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex.,Rasool S, Veyron S, Soya N, Eldeeb MA, Lukacs GL, Fon EA, Trempe JF Mol Cell. 2021 Nov 26. pii: S1097-2765(21)00991-6. doi:, 10.1016/j.molcel.2021.11.012. PMID:34875213[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||