View source for 6kgi


==RLGS-yUbr1 Ubr box==
<StructureSection load='6kgi' size='340' side='right'caption='[[6kgi]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KGI 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]] 1.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6kgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgi OCA], [https://pdbe.org/6kgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kgi RCSB], [https://www.ebi.ac.uk/pdbsum/6kgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBR1_YEAST UBR1_YEAST] Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-degron pathway, formerly the N-end rule pathway, is a protein degradation process that determines the half-life of proteins based on their N-terminal residues. In contrast to the well-established in vivo studies over decades, in vitro studies of this pathway, including biochemical characterization and high-resolution structures, are relatively limited. In this study, we have developed a unique fusion technique using microtubule-associated protein 1A/1B light chain 3B, a key marker protein of autophagy, to tag the N-terminus of the proteins involved in the N-degron pathway, which enables high yield of homogeneous target proteins with variable N-terminal residues for diverse biochemical studies including enzymatic and binding assays and substrate identification. Intriguingly, crystallization showed a markedly enhanced probability, even for the N-degron complexes. To validate our results, we determined the structures of select proteins in the N-degron pathway and compared them to the PDB-deposited proteins. Furthermore, several biochemical applications of this technique were introduced. Therefore, this technique can be used as a general tool for the in vitro study of the N-degron pathway.

Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway.,Kim L, Kwon DH, Heo J, Park MR, Song HK J Biol Chem. 2020 Jan 9. pii: RA119.010912. doi: 10.1074/jbc.RA119.010912. PMID:31919097<ref>PMID:31919097</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kgi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Heo J]]
[[Category: Kim L]]
[[Category: Kwon DH]]
[[Category: Song HK]]