8HTE

Crystal structure of an effector mutant in complex with ubiquitin

8HTE の概要

• エントリーDOI: 10.2210/pdb8hte/pdb
• 分子名称: NAD(+)--protein-threonine ADP-ribosyltransferase, Ubiquitin, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: transferase, ubiquitination
• 由来する生物種: Chromobacterium violaceum ATCC 12472; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35647.43

構造登録者

Tan, J.,Wang, X.,Zhou, Y.,Zhu, Y. (登録日: 2022-12-21, 公開日: 2023-11-22, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.307 Å)