Allosteric control of Ubp6 and the proteasome via a bidirectional switch - Hung, Ka Ying Sharon; Klumpe, Sven; Eisele, Markus R.; Elsasser, Suzanne; Tian, Geng; Sun, Shuangwu; Moroco, Jamie A.; Cheng, Tat Cheung; Joshi, Tapan; Seibel, Timo; Van Dalen, Duco; Feng, Xin-Hua; et al. (Nature communications, 2022)
Keywords: 101/28; 101/58; 631/45/474/2085; 631/45/474/2289; 631/535/1258/1259; 82/80; 82/83; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Allosteric properties; Catalytic Domain; Conformation; Cryoelectron Microscopy; Cytoplasm; Endopeptidases - chemistry; Endopeptidases - genetics; Endopeptidases - metabolism; Grooves; Humanities and Social Sciences; multidisciplinary; Mutation; Proteasome Endopeptidase Complex - chemistry; Proteasome Endopeptidase Complex - genetics; Proteasome Endopeptidase Complex - metabolism; Proteasomes; Protein Conformation; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Science; Science (multidisciplinary); Substrates; Topology; Ubiquitin; Ubiquitin - metabolism; Ubiquitinated Proteins - metabolism; Yeast