View source for 6lhn


==RLGSGG-AtPRT6 UBR box==
<StructureSection load='6lhn' size='340' side='right'caption='[[6lhn]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LHN 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]] 2.5&#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=6lhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lhn OCA], [https://pdbe.org/6lhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lhn RCSB], [https://www.ebi.ac.uk/pdbsum/6lhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lhn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRT6_ARATH PRT6_ARATH] Ubiquitin protein ligase which is a component of the N-end rule pathway with arginine specificity, and functions with the arginyltransferases ATE1 and ATE2. 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 (PubMed:17572409, PubMed:19255443, PubMed:19620738, PubMed:22020282). Does not participate in degradation of proteins with N-terminal Phe or Leu (PubMed:17572409). The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination (PubMed:19255443). The N-end rule pathway regulates various aspects of leaf and shoot development (PubMed:19620738). Involved in the ubiquitination and subsequent degradation of RAP2-12, an activator of hypoxic gene expression. The ubiquitination occurs after the N-arginylation of RAP2-12 by ATE1 or ATE2 under aerobic conditions (PubMed:22020282). The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato (PubMed:27173012, PubMed:30117535). Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity (PubMed:27173012). Controls the expression of specific defense-response genes, activates the synthesis pathway for the phytoalexin camalexin, and influences basal resistance to the hemibiotroph pathogen Pseudomonas syringae pv tomato (PubMed:30117535). Coordinates the mobilization of seed storage reserves and regulates the abundance and activities of several proteases following seed germination (PubMed:29168982).<ref>PMID:17572409</ref> <ref>PMID:19255443</ref> <ref>PMID:19620738</ref> <ref>PMID:22020282</ref> <ref>PMID:27173012</ref> <ref>PMID:29168982</ref> <ref>PMID:30117535</ref> 
<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 6lhn" style="background-color:#fffaf0;"></div>

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