Structural highlights
Function
PUP_CORGL Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.[HAMAP-Rule:MF_02106][1] PAFA_CORGL
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ozcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E. Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. Nat Commun. 2012 Aug 21;3:1014. doi: 10.1038/ncomms2009. PMID:22910360 doi:http://dx.doi.org/10.1038/ncomms2009
- ↑ 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
