8HTD

Crystal structure of an effector from Chromobacterium violaceum in complex with ubiquitin

Summary for 8HTD

• Entry DOI: 10.2210/pdb8htd/pdb
• Descriptor: NAD(+)--protein-threonine ADP-ribosyltransferase, Ubiquitin (3 entities in total)
• Functional Keywords: transferase, ubiquitination
• Biological source: Chromobacterium violaceum ATCC 12472; More
• Total number of polymer chains: 2
• Total formula weight: 34647.71

Authors

Tan, J.,Wang, X.,Zhou, Y.,Zhu, Y. (deposition date: 2022-12-21, release date: 2023-11-22, Last modification date: 2024-10-09)

Primary citation

Tan, J.,Xu, Y.,Wang, X.,Yan, F.,Xian, W.,Liu, X.,Chen, Y.,Zhu, Y.,Zhou, Y.
Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs.
Nat.Chem.Biol., 20:463-472, 2024

PubMed Abstract: Ubiquitination plays essential roles in eukaryotic cellular processes. The effector protein CteC from Chromobacterium violaceum blocks host ubiquitination by mono-ADP-ribosylation of ubiquitin (Ub) at residue T66. However, the structural basis for this modification is unknown. Here we report three crystal structures of CteC in complexes with Ub, NAD or ADP-ribosylated Ub, which represent different catalytic states of CteC in the modification. CteC adopts a special 'D-E' catalytic motif for catalysis and binds NAD in a half-ligand binding mode. The specific recognition of Ub by CteC is determined by a relatively separate Ub-targeting domain and a long loop L6, not the classic ADP-ribosylating turn-turn loop. Structural analyses with biochemical results reveal that CteC represents a large family of poly (ADP-ribose) polymerase (PARP)-like ADP-ribosyltransferases, which harbors chimeric features from the R-S-E and H-Y-E classes of ADP-ribosyltransferases. The family of CteC-like ADP-ribosyltransferases has a common 'D-E' catalytic consensus and exists extensively in bacteria and eukaryotic microorganisms.

PubMed: 37945894
DOI: 10.1038/s41589-023-01475-3

Experimental method

X-RAY DIFFRACTION (1.848 Å)