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| <StructureSection load='6b7p' size='340' side='right'caption='[[6b7p]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='6b7p' size='340' side='right'caption='[[6b7p]], [[Resolution|resolution]] 1.51Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <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> | | <table><tr><td colspan='2'>[[6b7p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. 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 [https://proteopedia.org/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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6b7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b7p OCA], [https://pdbe.org/6b7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b7p RCSB], [https://www.ebi.ac.uk/pdbsum/6b7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b7p ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q6RCQ7_LEGPN Q6RCQ7_LEGPN] |
| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 6b7p" style="background-color:#fffaf0;"></div>
| |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 33152]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Akturk, A]]
| | [[Category: Legionella pneumophila]] |
| [[Category: Mao, Y]]
| | [[Category: Akturk A]] |
| [[Category: Wasilko, J]]
| | [[Category: Mao Y]] |
| [[Category: Adpr-ub]]
| | [[Category: Wasilko J]] |
| [[Category: Cell invasion]]
| |
| [[Category: Legionella]] | |
| [[Category: Phosphodiesterase]] | |
| [[Category: Pr-ub]] | |
| [[Category: Sded]] | |
| [[Category: Ubiquitin]]
| |
