5zq2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
m Protected "5zq2" [edit=sysop:move=sysop]
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 5zq2 is ON HOLD
==SidE apo form==
<StructureSection load='5zq2' size='340' side='right'caption='[[5zq2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zq2]] 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=5ZQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZQ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.704&#8491;</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=5zq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zq2 OCA], [https://pdbe.org/5zq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zq2 RCSB], [https://www.ebi.ac.uk/pdbsum/5zq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zq2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6BBR6_LEGPN Q6BBR6_LEGPN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitination constitutes one of the most important signaling mechanisms in eukaryotes. Conventional ubiquitination is catalyzed by the universally conserved E1-E2-E3 three-enzyme cascade in an ATP-dependent manner. The newly identified SidE family effectors of the pathogen Legionella pneumophila ubiquitinate several human proteins by a different mechanism without engaging any of the conventional ubiquitination machinery. We now report the crystal structures of SidE alone and in complex with ubiquitin, NAD, and ADP-ribose, thereby capturing different conformations of SidE before and after ubiquitin and ligand binding. The structures of ubiquitin bound to both mART and PDE domains reveal several unique features of the two reaction steps catalyzed by SidE. Further, the structural and biochemical results demonstrate that SidE family members do not recognize specific structural folds of the substrate proteins. Our studies provide both structural explanations for the functional observations and new insights into the molecular mechanisms of this non-canonical ubiquitination machinery.


Authors:  
Structural Insights into Non-canonical Ubiquitination Catalyzed by SidE.,Wang Y, Shi M, Feng H, Zhu Y, Liu S, Gao A, Gao P Cell. 2018 May 17;173(5):1231-1243.e16. doi: 10.1016/j.cell.2018.04.023. Epub, 2018 May 3. PMID:29731171<ref>PMID:29731171</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5zq2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila]]
[[Category: Gao A]]
[[Category: Gao P]]
[[Category: Wang Y]]
Retrieved from "https://proteopedia.org/5zq2"