6SWY

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

Summary for 6SWY

• Entry DOI: 10.2210/pdb6swy/pdb
• EMDB information: 10326 10327 10328 10329 10330 10331 10332 10333
• Descriptor: Vacuolar import and degradation protein 28, Glucose-induced degradation protein 8, Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30, ... (5 entities in total)
• Functional Keywords: suppressed, suppreseed, ligase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 5
• Total formula weight: 370481.07

Authors

Qiao, S.,Prabu, J.R.,Schulman, B.A. (deposition date: 2019-09-24, release date: 2019-11-20, Last modification date: 2024-07-10)

Primary citation

Qiao, S.,Langlois, C.R.,Chrustowicz, J.,Sherpa, D.,Karayel, O.,Hansen, F.M.,Beier, V.,von Gronau, S.,Bollschweiler, D.,Schafer, T.,Alpi, A.F.,Mann, M.,Rajan Prabu, J.,Schulman, B.A.
Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly
Mol.Cell, 77:1-14, 2020

PubMed Abstract: 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 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), which awaits a glucose-induced substrate receptor to form the active GID. Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GID enables anticipating and ultimately binding various N-degron-targeting (i.e., "N-end rule") substrate receptors, while the GID 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.

PubMed: 31708416
DOI: 10.1016/j.molcel.2019.10.009

Experimental method

ELECTRON MICROSCOPY (3.2 Å)