Crystallization and preliminary X-ray analysis of Atg3.
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Summary
Crystals of Saccharomyces cerevisiae Atg3, an E2-like enzyme that catalyzes the conjugation reaction between Atg8 and PE, have been obtained by the sitting-drop vapour-diffusion method using ammonium sulfate and lithium sulfate as precipitants.
- Type
- article
- Published
- 2006-10-01
- Cited by
- 7
- References
- 10
- Access
- Open access
- OpenAlex
- https://openalex.org/W1988438459
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23733029
Keywords
Crystallization, Materials science, X-ray, Crystallography, Chemistry
References
- A ubiquitin-like system mediates protein lipidation
- The ubiquitin system.
- Solvent content of protein crystals.
- The Reversible Modification Regulates the Membrane-Binding State of Apg8/Aut7 Essential for Autophagy and the Cytoplasm to Vacuole Targeting Pathway
- In Vivo and in Vitro Reconstitution of Atg8 Conjugation Essential for Autophagy*
- Structural Basis for the Specificity and Catalysis of Human Atg4B Responsible for Mammalian Autophagy*
- Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy.
Cited by
- The Crystal Structure of Atg3, an Autophagy-related Ubiquitin Carrier Protein (E2) Enzyme that Mediates Atg8 Lipidation*
- Atg12–Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site
- Structural basis of Atg8 activation by a homodimeric E1, Atg7.
- Illuminating intercellular autophagy: A comprehensive review of cell non-autonomous autophagy.
- Phase separation promotes Atg8 lipidation for autophagy progression
- Phase separation promotes Atg8 lipidation and vesicle condensation for autophagy progression
- Illuminating Intercellular Autophagy: A Comprehensive Review of Cell Non-Autonomous Autophagy
- Illuminating Intercellular Autophagy: A Comprehensive Review of Cell Non-Autonomous Autophagy
- Crystallographic Studies on Autophagy-Related Proteins
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