7ns5: Difference between revisions
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==Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1)== | ==Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1)== | ||
<StructureSection load='7ns5' size='340' side='right'caption='[[7ns5]]' scene=''> | <StructureSection load='7ns5' size='340' side='right'caption='[[7ns5]], [[Resolution|resolution]] 1.95Å' 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=7NS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NS5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ns5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NS5 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=7ns5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ns5 OCA], [https://pdbe.org/7ns5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ns5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ns5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ns5 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </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=7ns5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ns5 OCA], [https://pdbe.org/7ns5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ns5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ns5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ns5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryoelectron microscopy (cryo-EM) structures show that, to bind the tetrameric substrate fructose-1,6-bisphosphatase (Fbp1), two minimally functional GID E3s assemble into the 20-protein Chelator-GID(SR4), which resembles an organometallic supramolecular chelate. The Chelator-GID(SR4) assembly avidly binds multiple Fbp1 degrons so that multiple Fbp1 protomers are simultaneously ubiquitylated at lysines near the allosteric and substrate binding sites. Importantly, key structural and biochemical features, including capacity for supramolecular assembly, are preserved in the human ortholog, the CTLH E3. Based on our integrative structural, biochemical, and cell biological data, we propose that higher-order E3 ligase assembly generally enables multipronged targeting, capable of simultaneously incapacitating multiple protomers and functionalities of oligomeric substrates. | |||
GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.,Sherpa D, Chrustowicz J, Qiao S, Langlois CR, Hehl LA, Gottemukkala KV, Hansen FM, Karayel O, von Gronau S, Prabu JR, Mann M, Alpi AF, Schulman BA Mol Cell. 2021 Apr 22. pii: S1097-2765(21)00220-3. doi:, 10.1016/j.molcel.2021.03.025. PMID:33905682<ref>PMID:33905682</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ns5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Fructose-bisphosphatase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chrustowicz J]] | [[Category: Chrustowicz, J]] | ||
[[Category: Prabu | [[Category: Prabu, J R]] | ||
[[Category: Schulman | [[Category: Schulman, B A]] | ||
[[Category: Sherpa D]] | [[Category: Sherpa, D]] | ||
[[Category: Cryoem]] | |||
[[Category: Ctlh]] | |||
[[Category: E3 ligase]] | |||
[[Category: Gid]] | |||
[[Category: Gluconeogenesis]] | |||
[[Category: Hydrolase]] | |||
[[Category: Metabolism]] | |||
[[Category: Supramolecular assembly]] | |||
[[Category: Ubiquitin]] | |||
Revision as of 12:41, 12 May 2021
Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1)Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1)
Structural highlights
Publication Abstract from PubMedHow are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryoelectron microscopy (cryo-EM) structures show that, to bind the tetrameric substrate fructose-1,6-bisphosphatase (Fbp1), two minimally functional GID E3s assemble into the 20-protein Chelator-GID(SR4), which resembles an organometallic supramolecular chelate. The Chelator-GID(SR4) assembly avidly binds multiple Fbp1 degrons so that multiple Fbp1 protomers are simultaneously ubiquitylated at lysines near the allosteric and substrate binding sites. Importantly, key structural and biochemical features, including capacity for supramolecular assembly, are preserved in the human ortholog, the CTLH E3. Based on our integrative structural, biochemical, and cell biological data, we propose that higher-order E3 ligase assembly generally enables multipronged targeting, capable of simultaneously incapacitating multiple protomers and functionalities of oligomeric substrates. GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.,Sherpa D, Chrustowicz J, Qiao S, Langlois CR, Hehl LA, Gottemukkala KV, Hansen FM, Karayel O, von Gronau S, Prabu JR, Mann M, Alpi AF, Schulman BA Mol Cell. 2021 Apr 22. pii: S1097-2765(21)00220-3. doi:, 10.1016/j.molcel.2021.03.025. PMID:33905682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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