Crystal structure of depupylase Dop in complex with Pup and AMP-PCP

PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE

Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.

The C-terminal ENLYFQ fragment is a leftover from TEV clevage site.

This is only the C-terminal half of the Pup protein.

100 mM Tris-acetate pH 7.0-8.5, 10 mM AMP-PCP, 40 mM MgCl2 and 0.75-1.0 M KH2PO4

Acidothermus cellulolyticus (strain ATCC 43068 / 11B)

depupylase, ATP hydrolysis, deamidase, Pup binding, HYDROLASE