6swy | pdb_00006swy

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

spinqualitylabelsall models 6swy, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6swy is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: UNK Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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). [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). [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). [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). [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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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