New structural clues to substrate specificity in the "ubiquitin system".
A 2.5 A crystal structure of a complex between the SUMO-conjugating enzyme Ubc9 and a protein substrate has yielded fresh insight into the specificity of protein modification by SUMO and other ubiquitin-like proteins.
Hochstrasser
Mark
M
Yale University, Department of Molecular Biophysics and Biochemistry, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06520, USA.
D018360:Crystallography, X-Ray; D008025:Ligases / Q000737:chemistry* / Q000378:metabolism; D046911:Macromolecular Substances; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D025841:Small Ubiquitin-Related Modifier Proteins / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D044763:Ubiquitin-Conjugating Enzymes; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D046911:Macromolecular Substances; D025841:Small Ubiquitin-Related Modifier Proteins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9