Barandun J Delley CL Ban N Weber-Ban E 2013 Prokaryotic ubiquitin-like protein (Pup) is covalently attached to target proteins by the ligase PafA, tagging substrates for proteasomal degradation. The crystal structure of Pup in complex with PafA, reported here, reveals that a long groove wrapping around the enzyme serves as a docking site for Pup. Upon binding, the C-terminal region of the intrinsically disordered Pup becomes ordered to form two helices connected by a linker, positioning the C-terminal glutamate in the active site of PafA. application/pdf https://sonar.ch/global/documents/139973 eng info:eu-repo/semantics/altIdentifier/doi/10.1021/ja4024012 info:eu-repo/semantics/altIdentifier/pmid/23601177 info:eu-repo/semantics/openAccess Journal of the American Chemical Society. - 2013 Corynebacterium glutamicum Crystallography, X-Ray Models, Molecular Protein Conformation Ubiquitin Ubiquitin-Protein Ligases Crystal structure of the complex between prokaryotic ubiquitin-like protein and its ligase PafA. http://purl.org/coar/resource_type/c_6501