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6.3.1.19: prokaryotic ubiquitin-like protein ligase

This is an abbreviated version!
For detailed information about prokaryotic ubiquitin-like protein ligase, go to the full flat file.

Word Map on EC 6.3.1.19

Reaction

ATP
+
[prokaryotic ubiquitin-like protein]-L-glutamate
 +
[protein]-L-lysine
=
ADP
 +
phosphate
 +
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine

Synonyms

PafA, proteasome accessory factor A, Pup ligase, Pup-protein ligase, Rv2097c, ubiquitin-like protein ligase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.1 Acid—ammonia (or amine) ligases (amide synthases)
                6.3.1.19 prokaryotic ubiquitin-like protein ligase

Crystallization

Crystallization on EC 6.3.1.19 - prokaryotic ubiquitin-like protein ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with ADP, protein (Pup) ligase PafA and the depupylase/deamidase Dop are are close structural homologues
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