Structural basis for adenylation and thioester bond formation in the ubiquitin E1

The ubiquitin (Ub) and Ub-like (Ubl) protein-conjugation cascade is initiated by E1 enzymes that catalyze Ub/Ubl activation through C-terminal adenylation, thioester bond formation with an E1 catalytic cysteine, and thioester bond transfer to Ub/Ubl E2 conjugating enzymes. Each of these reactions is...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2019-07, Vol.116 (31), p.15475-15484
Hauptverfasser:	Hann, Zachary S., Ji, Cheng, Olsen, Shaun K., Lu, Xuequan, Lux, Michaelyn C., Tan, Derek S., Lima, Christopher D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenine - chemistry Adenylation Animals BASIC BIOLOGICAL SCIENCES Biochemical analysis biochemistry Biological Sciences Bonding Catalysis Catalytic Domain Conjugation Conserved Sequence Cysteine Diphosphates - metabolism DNA Mutational Analysis Enzymes Esters - chemistry PNAS Plus Protein Conformation Schizosaccharomyces - enzymology Schizosaccharomyces pombe Proteins - chemistry Schizosaccharomyces pombe Proteins - metabolism Sulfhydryl Compounds - chemistry thioester Ubiquitin Ubiquitin - metabolism Ubiquitin-Activating Enzymes - chemistry Ubiquitin-Activating Enzymes - metabolism x-ray
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