6b7p

<StructureSection load='6b7p' size='340' side='right' caption='[[6b7p]], [[Resolution|resolution]] 1.51&Aring;' scene=''>

<table><tr><td colspan='2'>[[6b7p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B7P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B7P FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6b7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b7p OCA], [http://pdbe.org/6b7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b7p RCSB], [http://www.ebi.ac.uk/pdbsum/6b7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b7p ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Ubiquitination is a post-translational modification that regulates many cellular processes in eukaryotes(1-4). 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(1,5). 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(6-8). 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 (9) 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.

 

Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector.,Akturk A, Wasilko DJ, Wu X, Liu Y, Zhang Y, Qiu J, Luo ZQ, Reiter KH, Brzovic PS, Klevit RE, Mao Y Nature. 2018 May;557(7707):729-733. doi: 10.1038/s41586-018-0147-6. Epub 2018 May, 23. PMID:29795346<ref>PMID:29795346</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<references/>

[[Category: Atcc 33152]]

[[Category: Cell invasion]]

[[Category: Legionella]]

[[Category: Phosphodiesterase]]

[[Category: Pr-ub]]

[[Category: Sded]]

[[Category: Ubiquitin]]