Structural highlights
7oyh is a 2 chain structure with sequence from Acidothermus cellulolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.75Å |
| Ligands: | ACT, ADP, EDO, MF4, MG, PEG, PGE, SO4 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
DOP_ACIC1 Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-terminal glutamine to glutamate in a variant of the prokaryotic ubiquitin-like protein Pup; however, since Pup from A.cellulolyticus possesses a C-terminal glutamate, this deamidase activity may be of no significance in vivo.[1]
Publication Abstract from PubMed
Pupylation is the post-translational modification of lysine side chains with prokaryotic ubiquitin-like protein (Pup) that targets proteins for proteasomal degradation in mycobacteria and other members of Actinobacteria. Pup ligase PafA and depupylase Dop are the two enzymes acting in this pathway. Although they share close structural and sequence homology indicative of a common evolutionary origin, they catalyze opposing reactions. Here, we report a series of high-resolution crystal structures of Dop in different functional states along the reaction pathway, including Pup-bound states in distinct conformations. In combination with biochemical analysis, the structures explain the role of the C-terminal residue of Pup in ATP hydrolysis, the process that generates the catalytic phosphate in the active site, and suggest a role for the Dop-loop as an allosteric sensor for Pup-binding and ATP cleavage.
Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.,Cui H, Muller AU, Leibundgut M, Tian J, Ban N, Weber-Ban E Nat Commun. 2021 Nov 17;12(1):6635. doi: 10.1038/s41467-021-26848-x. PMID:34789727[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ozcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E. Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. Nat Commun. 2012 Aug 21;3:1014. doi: 10.1038/ncomms2009. PMID:22910360 doi:https://dx.doi.org/10.1038/ncomms2009
- ↑ Cui H, Müller AU, Leibundgut M, Tian J, Ban N, Weber-Ban E. Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation. Nat Commun. 2021 Nov 17;12(1):6635. PMID:34789727 doi:10.1038/s41467-021-26848-x
