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6swy

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==Structure of active GID E3 ubiquitin ligase complex minus Gid2 and delta Gid9 RING domain==
==Structure of active GID E3 ubiquitin ligase complex minus Gid2 and delta Gid9 RING domain==
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<StructureSection load='6swy' size='340' side='right'caption='[[6swy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<SX load='6swy' size='340' side='right' viewer='molstar' caption='[[6swy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6swy]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SWY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6swy]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SWY FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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</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=6swy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6swy OCA], [https://pdbe.org/6swy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6swy RCSB], [https://www.ebi.ac.uk/pdbsum/6swy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6swy ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6swy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6swy OCA], [http://pdbe.org/6swy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6swy RCSB], [http://www.ebi.ac.uk/pdbsum/6swy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6swy ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GID4_YEAST GID4_YEAST]] Substrate-recognition component of the GID complex, a multisubunit ubiquitin ligase that targets enzymes involved in gluconeogenesis for proteasomal degradation when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:18508925, PubMed:28126757). Specific for substrates with an N-terminal Pro (Pro/N-degron), including FBP1, ICL1 and MDH2 (PubMed:28126757). Has high affinity for the N-terminal sequence Pro-Thr-Leu-Val, and can bind peptides with an N-terminal sequence of the type Pro-[Gly,Ala,Ser,Thr,Asp,Asn,Tyr,His]-[Ala,Val,Leu,Ile,Lys,Arg]-[Val,Cys,Pro,Leu,Ile,Trp] (PubMed:28126757). Required for vacuolar degradation of FBP1 when cells are shifted to glucose-containing medium, probably by targeting FBP1-containing vesicles to the vacuole, but is not required for FBP1 sequestration in cytoplasmic vesicles (PubMed:9508768).<ref>PMID:12686616</ref> <ref>PMID:18508925</ref> <ref>PMID:28126757</ref> <ref>PMID:9508768</ref> [[http://www.uniprot.org/uniprot/VID28_YEAST VID28_YEAST]] Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616).<ref>PMID:12686616</ref> [[http://www.uniprot.org/uniprot/VID30_YEAST VID30_YEAST]] Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:9737955, PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:12686616, PubMed:22645139, PubMed:28126757).<ref>PMID:12686616</ref> <ref>PMID:22645139</ref> <ref>PMID:28126757</ref> <ref>PMID:9737955</ref> [[http://www.uniprot.org/uniprot/GID8_YEAST GID8_YEAST]] Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616). Required also for cell cycle progression. Positively controls G1 and the timing of START (PubMed:15590836).<ref>PMID:12686616</ref> <ref>PMID:15590836</ref> [[http://www.uniprot.org/uniprot/FYV10_YEAST FYV10_YEAST]] Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:22044534). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616, PubMed:22044534). May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin (PubMed:12663529).<ref>PMID:12663529</ref> <ref>PMID:12686616</ref> <ref>PMID:22044534</ref>
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[[https://www.uniprot.org/uniprot/VID28_YEAST VID28_YEAST]] Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616).<ref>PMID:12686616</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Prabu, J R]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Qiao, S]]
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[[Category: Prabu JR]]
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[[Category: Schulman, B A]]
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[[Category: Qiao S]]
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[[Category: Ligase]]
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[[Category: Schulman BA]]
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[[Category: Suppreseed]]
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[[Category: Suppressed]]
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Current revision

Structure of active GID E3 ubiquitin ligase complex minus Gid2 and delta Gid9 RING domain

6swy, resolution 3.20Å

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