5lp0: Difference between revisions

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New page: '''Unreleased structure''' The entry 5lp0 is ON HOLD until Paper Publication Authors: Levin-Kravets, O., Prag, G. Description: CRYSTAL STRUCTURE OF THE ZEBRA FISH ENTH DOMAIN FROM EPSI...
 
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'''Unreleased structure'''


The entry 5lp0 is ON HOLD  until Paper Publication
==CRYSTAL STRUCTURE OF THE ZEBRA FISH ENTH DOMAIN FROM EPSIN1 IN 1.41 ANGSTROM RESOLUTION==
<StructureSection load='5lp0' size='340' side='right'caption='[[5lp0]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lp0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LP0 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]] 1.41&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5lp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lp0 OCA], [https://pdbe.org/5lp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lp0 RCSB], [https://www.ebi.ac.uk/pdbsum/5lp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lp0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1Q5Z9_DANRE F1Q5Z9_DANRE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
About one-third of the eukaryotic proteome undergoes ubiquitylation, but the enzymatic cascades leading to substrate modification are largely unknown. We present a genetic selection tool that utilizes Escherichia coli, which lack deubiquitylases, to identify interactions along ubiquitylation cascades. Coexpression of split antibiotic resistance protein tethered to ubiquitin and ubiquitylation target together with a functional ubiquitylation apparatus results in a covalent assembly of the resistance protein, giving rise to bacterial growth on selective media. We applied the selection system to uncover an E3 ligase from the pathogenic bacteria EHEC and to identify the epsin ENTH domain as an ultraweak ubiquitin-binding domain. The latter was complemented with a structure-function analysis of the ENTH-ubiquitin interface. We also constructed and screened a yeast fusion library, discovering Sem1 as a novel ubiquitylation substrate of Rsp5 E3 ligase. Collectively, our selection system provides a robust high-throughput approach for genetic studies of ubiquitylation cascades and for small-molecule modulator screening.


Authors: Levin-Kravets, O., Prag, G.
A bacterial genetic selection system for ubiquitylation cascade discovery.,Levin-Kravets O, Tanner N, Shohat N, Attali I, Keren-Kaplan T, Shusterman A, Artzi S, Varvak A, Reshef Y, Shi X, Zucker O, Baram T, Katina C, Pilzer I, Ben-Aroya S, Prag G Nat Methods. 2016 Oct 3. doi: 10.1038/nmeth.4003. PMID:27694912<ref>PMID:27694912</ref>


Description: CRYSTAL STRUCTURE OF THE ZEBRA FISH ENTH DOMAIN FROM EPSIN1 IN 1.41 ANGSTROM RESOLUTION
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Prag, G]]
<div class="pdbe-citations 5lp0" style="background-color:#fffaf0;"></div>
[[Category: Levin-Kravets, O]]
 
==See Also==
*[[Epsin|Epsin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Levin-Kravets O]]
[[Category: Prag G]]

Latest revision as of 18:38, 18 October 2023

CRYSTAL STRUCTURE OF THE ZEBRA FISH ENTH DOMAIN FROM EPSIN1 IN 1.41 ANGSTROM RESOLUTION

5lp0, resolution 1.41Å

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