4bjr

Crystal structure of the complex between Prokaryotic Ubiquitin-like Protein Pup and its Ligase PafA

spinqualitylabelsall models 4bjr, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bjr is a 2 chain structure with sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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