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| | <SX load='6swy' size='340' side='right' viewer='molstar' caption='[[6swy]], [[Resolution|resolution]] 3.20Å' scene=''> | | <SX load='6swy' size='340' side='right' viewer='molstar' caption='[[6swy]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6swy]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_yjm1133 Saccharomyces cerevisiae yjm1133]. 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> | + | <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> |
| - | </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> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VID28, GID5, YIL017C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1294333 Saccharomyces cerevisiae YJM1133]), GID8, DCR1, YMR135C, YM9375.04C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), VID30, GID1, YGL227W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), VID24, GID4, YBR105C, YBR0834 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), FYV10, GID9, YIL097W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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> [[https://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> [[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> [[https://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> [[https://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>
| + | [[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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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Saccharomyces cerevisiae yjm1133]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Prabu, J R]] | + | [[Category: Prabu JR]] |
| - | [[Category: Qiao, S]] | + | [[Category: Qiao S]] |
| - | [[Category: Schulman, B A]] | + | [[Category: Schulman BA]] |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Suppreseed]]
| + | |
| - | [[Category: Suppressed]]
| + | |
| Structural highlights
Function
[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).[1]
Publication Abstract from PubMed
Cells respond to environmental changes by toggling metabolic pathways, preparing for homeostasis, and anticipating future stresses. For example, in Saccharomyces cerevisiae, carbon stress-induced gluconeogenesis is terminated upon glucose availability, a process that involves the multiprotein E3 ligase GID(SR4) recruiting N termini and catalyzing ubiquitylation of gluconeogenic enzymes. Here, genetics, biochemistry, and cryoelectron microscopy define molecular underpinnings of glucose-induced degradation. Unexpectedly, carbon stress induces an inactive anticipatory complex (GID(Ant)), which awaits a glucose-induced substrate receptor to form the active GID(SR4). Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GID(Ant) enables anticipating and ultimately binding various N-degron-targeting (i.e., "N-end rule") substrate receptors, while the GID(SR4) E3 forms a clamp-like structure juxtaposing substrate lysines with the ubiquitylation active site. The data reveal evolutionarily conserved GID complexes as a family of multisubunit E3 ubiquitin ligases responsive to extracellular stimuli.
Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly.,Qiao S, Langlois CR, Chrustowicz J, Sherpa D, Karayel O, Hansen FM, Beier V, von Gronau S, Bollschweiler D, Schafer T, Alpi AF, Mann M, Prabu JR, Schulman BA Mol Cell. 2019 Nov 1. pii: S1097-2765(19)30769-5. doi:, 10.1016/j.molcel.2019.10.009. PMID:31708416[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Regelmann J, Schule T, Josupeit FS, Horak J, Rose M, Entian KD, Thumm M, Wolf DH. Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell. 2003 Apr;14(4):1652-63. doi: 10.1091/mbc.e02-08-0456. PMID:12686616 doi:http://dx.doi.org/10.1091/mbc.e02-08-0456
- ↑ Qiao S, Langlois CR, Chrustowicz J, Sherpa D, Karayel O, Hansen FM, Beier V, von Gronau S, Bollschweiler D, Schafer T, Alpi AF, Mann M, Prabu JR, Schulman BA. Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. Mol Cell. 2019 Nov 1. pii: S1097-2765(19)30769-5. doi:, 10.1016/j.molcel.2019.10.009. PMID:31708416 doi:http://dx.doi.org/10.1016/j.molcel.2019.10.009
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