3nit

<table><tr><td colspan='2'>[[3nit]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NIT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nih|3nih]], [[3nii|3nii]], [[3nij|3nij]], [[3nik|3nik]], [[3nil|3nil]], [[3nim|3nim]], [[3nin|3nin]], [[3nis|3nis]]</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=3nit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nit OCA], [http://pdbe.org/3nit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nit RCSB], [http://www.ebi.ac.uk/pdbsum/3nit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nit ProSAT]</span></td></tr>

[[http://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.

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== Publication Abstract from PubMed ==

The N-end rule pathway is a regulated proteolytic system that targets proteins containing destabilizing N-terminal residues (N-degrons) for ubiquitination and proteasomal degradation in eukaryotes. The N-degrons of type 1 substrates contain an N-terminal basic residue that is recognized by the UBR box domain of the E3 ubiquitin ligase UBR1. We describe structures of the UBR box of Saccharomyces cerevisiae UBR1 alone and in complex with N-degron peptides, including that of the cohesin subunit Scc1, which is cleaved and targeted for degradation at the metaphase-anaphase transition. The structures reveal a previously unknown protein fold that is stabilized by a novel binuclear zinc center. N-terminal arginine, lysine or histidine side chains of the N-degron are coordinated in a multispecific binding pocket. Unexpectedly, the structures together with our in vitro biochemical and in vivo pulse-chase analyses reveal a previously unknown modulation of binding specificity by the residue at position 2 of the N-degron.

Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases.,Choi WS, Jeong BC, Joo YJ, Lee MR, Kim J, Eck MJ, Song HK Nat Struct Mol Biol. 2010 Sep 12. PMID:20835240<ref>PMID:20835240</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3nit" style="background-color:#fffaf0;"></div>

*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]

[[Category: Atcc 18824]]

[[Category: Choi, W S]]

[[Category: Jeong, B C]]

[[Category: Lee, M R]]

[[Category: Song, H K]]

[[Category: Zinc-binding protein]]