Structural highlights
Publication Abstract from PubMed
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.
Crystal Structure of the Complex between Prokaryotic Ubiquitin-like Protein and Its Ligase PafA.,Barandun J, Delley CL, Ban N, Weber-Ban E J Am Chem Soc. 2013 Apr 23. PMID:23601177[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barandun J, Delley CL, Ban N, Weber-Ban E. Crystal Structure of the Complex between Prokaryotic Ubiquitin-like Protein and Its Ligase PafA. J Am Chem Soc. 2013 Apr 23. PMID:23601177 doi:10.1021/ja4024012
