Literature summary for 6.3.1.19 extracted from

Barandun, J.; Delley, C.L.; Ban, N.; Weber-Ban, E.
Crystal structure of the complex between prokaryotic ubiquitin-like protein and its ligase PafA (2013), J. Am. Chem. Soc., 135, :6794-6797.

Crystallization (Commentary)

Crystallization (Comment)	Organism
the enzyme from Corynebacterium glutamicum is C-terminally fused with Pup or N-terminally truncated fragments of prokaryotic ubiquitin-like protein (Pup) from the same organism. Crystals are obtained only with the shortest fragment tested, PupE38-64. The crystal structure of Pup in complex with the enzyme, 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	Corynebacterium glutamicum

Crystallization (Comment)

Organism

the enzyme from Corynebacterium glutamicum is C-terminally fused with Pup or N-terminally truncated fragments of prokaryotic ubiquitin-like protein (Pup) from the same organism. Crystals are obtained only with the shortest fragment tested, PupE38-64. The crystal structure of Pup in complex with the enzyme, 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

Corynebacterium glutamicum

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	Q8NQE0	-	-
Corynebacterium glutamicum DSM 20300	Q8NQE0	-	-

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Release 2023.1 (January 2023)