7ep4: Difference between revisions
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==Crystal structure of ZER1 bound to GFLH degron== | ==Crystal structure of ZER1 bound to GFLH degron== | ||
<StructureSection load='7ep4' size='340' side='right'caption='[[7ep4]]' scene=''> | <StructureSection load='7ep4' size='340' side='right'caption='[[7ep4]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EP4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ep4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EP4 FirstGlance]. <br> | ||
</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=7ep4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ep4 OCA], [https://pdbe.org/7ep4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ep4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ep4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ep4 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07Å</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=7ep4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ep4 OCA], [https://pdbe.org/7ep4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ep4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ep4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ep4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ZER1_HUMAN ZER1_HUMAN] Serves as substrate adapter subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC (PubMed:17304241, PubMed:31273098). Acts redudantly with ZYG11B to target substrates bearing N-terminal glycine degrons for proteasomal degradation (PubMed:33093214). Involved in the clearance of proteolytic fragments generated by caspase cleavage during apoptosis since N-terminal glycine degrons are strongly enriched at caspase cleavage sites. Also important in the quality control of protein N-myristoylation in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation (PubMed:31273098).<ref>PMID:17304241</ref> <ref>PMID:31273098</ref> <ref>PMID:33093214</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-degron pathways are a set of proteolytic systems that target the N-terminal destabilizing residues of substrates for proteasomal degradation. Recently, the Gly/N-degron pathway has been identified as a new branch of the N-degron pathway. The N-terminal glycine degron (Gly/N-degron) is recognized by ZYG11B and ZER1, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2). Here we present the crystal structures of ZYG11B and ZER1 bound to various Gly/N-degrons. The structures reveal that ZYG11B and ZER1 utilize their armadillo (ARM) repeats forming a deep and narrow cavity to engage mainly the first four residues of Gly/N-degrons. The alpha-amino group of the Gly/N-degron is accommodated in an acidic pocket by five conserved hydrogen bonds. These structures, together with biochemical studies, decipher the molecular basis for the specific recognition of the Gly/N-degron by ZYG11B and ZER1, providing key information for future structure-based chemical probe design. | |||
Molecular basis for recognition of Gly/N-degrons by CRL2(ZYG11B) and CRL2(ZER1).,Yan X, Li Y, Wang G, Zhou Z, Song G, Feng Q, Zhao Y, Mi W, Ma Z, Dong C Mol Cell. 2021 Jun 23. pii: S1097-2765(21)00457-3. doi:, 10.1016/j.molcel.2021.06.010. PMID:34214466<ref>PMID:34214466</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ep4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li Y]] | [[Category: Li Y]] | ||
[[Category: Yan X]] | [[Category: Yan X]] | ||