4BJR

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

Summary for 4BJR

• Entry DOI: 10.2210/pdb4bjr/pdb
• Descriptor: PUP--PROTEIN LIGASE, PROKARYOTIC UBIQUITIN-LIKE PROTEIN PUP, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: ligase, prokaryotic proteasome
• Biological source: CORYNEBACTERIUM GLUTAMICUM
• Total number of polymer chains: 2
• Total formula weight: 116098.93

Authors

Barandun, J.,Delley, C.L.,Ban, N.,Weber-Ban, E. (deposition date: 2013-04-19, release date: 2013-05-01, Last modification date: 2023-12-20)

Primary citation

Barandun, J.,Delley, C.L.,Ban, N.,Weber-Ban, E.
Crystal Structure of the Complex between Prokaryotic Ubiquitin-Like Protein Pup and its Ligase Pafa.
J.Am.Chem.Soc., 135:6794-, 2013

PubMed Abstract: 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.

PubMed: 23601177
DOI: 10.1021/JA4024012

Experimental method

X-RAY DIFFRACTION (2.8 Å)