7xyt - Revision history

OCA at 09:39, 14 February 2024

2024-02-14T09:39:49Z

←Older revision		Revision as of 09:39, 14 February 2024
Line 9:		Line 9:
	== Function ==		== 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>		[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 pathway plays an important role in the protein quality control and maintenance of cellular protein homeostasis. ZER1 and ZYG11B, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2), recognize N-terminal (Nt) glycine degrons and participate in the Nt-myristoylation quality control through the Gly/N-degron pathway. Here we show that ZER1 and ZYG11B can also recognize small Nt-residues other than glycine. Specifically, ZER1 binds better to Nt-Ser, -Ala, -Thr and -Cys than to -Gly, while ZYG11B prefers Nt-Gly but also has the capacity to recognize Nt-Ser, -Ala and -Cys in vitro. We found that Nt-Ser, -Ala and -Cys undergo Nt-acetylation catalyzed by Nt-acetyltransferase (NAT), thereby shielding them from recognition by ZER1/ZYG11B in cells. Instead, ZER1/ZYG11B readily targets a selection of small Nt-residues lacking Nt-acetylation for degradation in NAT-deficient cells, implicating its role in the Nt-acetylation quality control. Furthermore, we present the crystal structures of ZER1 and ZYG11B bound to various small Nt-residues and uncover the molecular mechanism of non-acetylated substrate recognition by ZER1 and ZYG11B.
-
-	CRL2(ZER1/ZYG11B) recognizes small N-terminal residues for degradation.,Li Y, Zhao Y, Yan X, Ye C, Weirich S, Zhang B, Wang X, Song L, Jiang C, Jeltsch A, Dong C, Mi W Nat Commun. 2022 Dec 10;13(1):7636. doi: 10.1038/s41467-022-35169-6. PMID:36496439<ref>PMID:36496439</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7xyt" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:07, 6 September 2023

2023-09-06T10:07:42Z

←Older revision		Revision as of 10:07, 6 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7xyt]] is a 4 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=7XYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XYT FirstGlance]. <br>		<table><tr><td colspan='2'>[[7xyt]] is a 4 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=7XYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XYT 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=7xyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xyt OCA], [https://pdbe.org/7xyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xyt RCSB], [https://www.ebi.ac.uk/pdbsum/7xyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xyt 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]] 1.5Å</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=7xyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xyt OCA], [https://pdbe.org/7xyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xyt RCSB], [https://www.ebi.ac.uk/pdbsum/7xyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xyt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 08:59, 28 December 2022

2022-12-28T08:59:24Z

←Older revision		Revision as of 08:59, 28 December 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7xyt is ~~ON HOLD~~	+	==Crystal structure of ZER1 bound to AFLH degron==
		+	<StructureSection load='7xyt' size='340' side='right'caption='[[7xyt]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[7xyt]] is a 4 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=7XYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XYT 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=7xyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xyt OCA], [https://pdbe.org/7xyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xyt RCSB], [https://www.ebi.ac.uk/pdbsum/7xyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xyt ProSAT]</span></td></tr>
		+	</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 pathway plays an important role in the protein quality control and maintenance of cellular protein homeostasis. ZER1 and ZYG11B, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2), recognize N-terminal (Nt) glycine degrons and participate in the Nt-myristoylation quality control through the Gly/N-degron pathway. Here we show that ZER1 and ZYG11B can also recognize small Nt-residues other than glycine. Specifically, ZER1 binds better to Nt-Ser, -Ala, -Thr and -Cys than to -Gly, while ZYG11B prefers Nt-Gly but also has the capacity to recognize Nt-Ser, -Ala and -Cys in vitro. We found that Nt-Ser, -Ala and -Cys undergo Nt-acetylation catalyzed by Nt-acetyltransferase (NAT), thereby shielding them from recognition by ZER1/ZYG11B in cells. Instead, ZER1/ZYG11B readily targets a selection of small Nt-residues lacking Nt-acetylation for degradation in NAT-deficient cells, implicating its role in the Nt-acetylation quality control. Furthermore, we present the crystal structures of ZER1 and ZYG11B bound to various small Nt-residues and uncover the molecular mechanism of non-acetylated substrate recognition by ZER1 and ZYG11B.

-	~~Authors: Dong, C~~., Yan, X., Li, Y.	+	CRL2(ZER1/ZYG11B) recognizes small N-terminal residues for degradation.,Li Y, Zhao Y, Yan X, Ye C, Weirich S, Zhang B, Wang X, Song L, Jiang C, Jeltsch A, Dong C, Mi W Nat Commun. 2022 Dec 10;13(1):7636. doi: 10.1038/s41467-022-35169-6. PMID:36496439<ref>PMID:36496439</ref>

-	~~Description: Crystal structure~~ of ~~ZER1 bound to AFLH degron~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: Dong, C]]	+	<div class="pdbe-citations 7xyt" style="background-color:#fffaf0;"></div>
-	[[Category: Li, Y]]	+	== References ==
-	[[Category: Yan, X]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Dong C]]
		+	[[Category: Li Y]]
		+	[[Category: Yan X]]

OCA at 05:51, 21 December 2022

2022-12-21T05:51:04Z

←Older revision		Revision as of 05:51, 21 December 2022
Line 5:		Line 5:
	Authors: Dong, C., Yan, X., Li, Y.		Authors: Dong, C., Yan, X., Li, Y.

-	Description: Crystal structure of ~~X2A~~	+	Description: Crystal structure of ZER1 bound to AFLH degron
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Yan, X]]
	[[Category: Dong, C]]		[[Category: Dong, C]]
	[[Category: Li, Y]]		[[Category: Li, Y]]
		+	[[Category: Yan, X]]

OCA: Protected "7xyt" [edit=sysop:move=sysop]

2022-06-08T04:06:05Z

Protected "7xyt" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:06, 8 June 2022

OCA: New page: '''Unreleased structure''' The entry 7xyt is ON HOLD Authors: Dong, C., Yan, X., Li, Y. Description: Crystal structure of X2A Category: Unreleased Structures Category: Yan, X [...

2022-06-08T04:06:04Z

New page: '''Unreleased structure''' The entry 7xyt is ON HOLD Authors: Dong, C., Yan, X., Li, Y. Description: Crystal structure of X2A Category: Unreleased Structures Category: Yan, X [...

New page

'''Unreleased structure'''

The entry 7xyt is ON HOLD

Authors: Dong, C., Yan, X., Li, Y.

Description: Crystal structure of X2A
[[Category: Unreleased Structures]]
[[Category: Yan, X]]
[[Category: Dong, C]]
[[Category: Li, Y]]