Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusi...

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Veröffentlicht in:	Nature (London) 2012-09, Vol.489 (7414), p.115-120
Hauptverfasser:	Plechanovová, Anna, Jaffray, Ellis G., Tatham, Michael H., Naismith, James H., Hay, Ronald T.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/337/474/2073 631/45/173 Animals Biocatalysis Biological and medical sciences Catalysis Catalytic Domain Crystalline structure Crystallography, X-Ray Enzymes Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans Hydrolysis Models, Molecular Molecular biophysics multidisciplinary Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Mutation Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Binding Protein Structure, Tertiary Proteins Rats Science Science (multidisciplinary) Structure in molecular biology Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Ubiquitin - chemistry Ubiquitin - genetics Ubiquitin - metabolism Ubiquitin-Conjugating Enzymes - chemistry Ubiquitin-Conjugating Enzymes - genetics Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism Ubiquitination Zinc Fingers
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