5YSI

SdeA mART-C domain EE/AA NCA complex

Summary for 5YSI

• Entry DOI: 10.2210/pdb5ysi/pdb
• Descriptor: Ubiquitinating/deubiquitinating enzyme SdeA, NICOTINAMIDE (3 entities in total)
• Functional Keywords: sdea, e3 ligase, legionella, hydrolase
• Biological source: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
• Total number of polymer chains: 1
• Total formula weight: 17045.74

Authors

Kim, L.,Kwon, D.H.,Song, H.K. (deposition date: 2017-11-14, release date: 2018-08-29, Last modification date: 2024-10-16)

Primary citation

Kim, L.,Kwon, D.H.,Kim, B.H.,Kim, J.,Park, M.R.,Park, Z.Y.,Song, H.K.
Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila
J. Mol. Biol., 430:2843-2856, 2018

PubMed Abstract: Conventional ubiquitylation occurs through an ATP-dependent three-enzyme cascade (E1, E2, and E3) that mediates the covalent conjugation of the C-terminus of ubiquitin to a lysine on the substrate. SdeA, which belongs to the SidE effector family of Legionella pneumophila, can transfer ubiquitin to endoplasmic reticulum-associated Rab-family GTPases in a manner independent of E1 and E2 enzymes. The novel ubiquitin-modifying enzyme SdeA utilizes NAD as a cofactor to attach ubiquitin to a serine residue of the substrate. Here, to elucidate the coupled enzymatic reaction of NAD+ hydrolysis and ADP-ribosylation of ubiquitin in SdeA, we characterized the mono-ADP-ribosyltransferase domain of SdeA and show that it consists of two sub-domains termed mART-N and mART-C. The crystal structure of the mART-C domain of SdeA was also determined in free form and in complex with NAD at high resolution. Furthermore, the spatial orientations of the N-terminal deubiquitylase, phosphodiesterase, mono-ADP-ribosyltransferase, and C-terminal coiled-coil domains within the 180-kDa full-length SdeA were determined. These results provide insight into the unusual ubiquitylation mechanism of SdeA and expand our knowledge on the structure-function of mono-ADP-ribosyltransferases.

PubMed: 29870726
DOI: 10.1016/j.jmb.2018.05.043

Experimental method

X-RAY DIFFRACTION (1.546 Å)