Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6B7P

Crystal structure of Legionella effector sdeD (lpg2509)

Summary for 6B7P
Entry DOI10.2210/pdb6b7p/pdb
DescriptorSdeD (2 entities in total)
Functional Keywordslegionella, ubiquitin, sded, adpr-ub, pr-ub, phosphodiesterase, cell invasion
Biological sourceLegionella pneumophila
Total number of polymer chains2
Total formula weight86878.03
Authors
Mao, Y.,Akturk, A.,Wasilko, J. (deposition date: 2017-10-04, release date: 2018-04-18, Last modification date: 2024-03-13)
Primary citationAkturk, A.,Wasilko, D.J.,Wu, X.,Liu, Y.,Zhang, Y.,Qiu, J.,Luo, Z.Q.,Reiter, K.H.,Brzovic, P.S.,Klevit, R.E.,Mao, Y.
Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector.
Nature, 557:729-733, 2018
Cited by
PubMed Abstract: Ubiquitination is a post-translational modification that regulates many cellular processes in eukaryotes. The conventional ubiquitination cascade culminates in a covalent linkage between the C terminus of ubiquitin (Ub) and a target protein, usually on a lysine side chain. Recent studies of the Legionella pneumophila SidE family of effector proteins revealed a ubiquitination method in which a phosphoribosyl ubiquitin (PR-Ub) is conjugated to a serine residue on substrates via a phosphodiester bond. Here we present the crystal structure of a fragment of the SidE family member SdeA that retains ubiquitination activity, and determine the mechanism of this unique post-translational modification. The structure reveals that the catalytic module contains two distinct functional units: a phosphodiesterase domain and a mono-ADP-ribosyltransferase domain. Biochemical analysis shows that the mono-ADP-ribosyltransferase domain-mediated conversion of Ub to ADP-ribosylated Ub (ADPR-Ub) and the phosphodiesterase domain-mediated ligation of PR-Ub to substrates are two independent activities of SdeA. Furthermore, we present two crystal structures of a homologous phosphodiesterase domain from the SidE family member SdeD in complexes with Ub and ADPR-Ub. The structures suggest a mechanism for how SdeA processes ADPR-Ub to PR-Ub and AMP, and conjugates PR-Ub to a serine residue in substrates. Our study establishes the molecular mechanism of phosphoribosyl-linked ubiquitination and will enable future studies of this unusual type of ubiquitination in eukaryotes.
PubMed: 29795346
DOI: 10.1038/s41586-018-0147-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.51 Å)
Structure validation

231029

건을2025-02-05부터공개중

PDB statisticsPDBj update infoContact PDBjnumon