6a0i - Revision history

OCA at 09:11, 22 November 2023

OCA — Wed, 22 Nov 2023 09:11:59 GMT

←Older revision		Revision as of 09:11, 22 November 2023
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	<StructureSection load='6a0i' size='340' side='right'caption='[[6a0i]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='6a0i' size='340' side='right'caption='[[6a0i]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6a0i]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6A0I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6a0i]] 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=6A0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A0I FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~, ~~<scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>~~</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]] 1.996Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~NTAN1 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6a0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0i OCA], [~~http~~://pdbe.org/6a0i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6a0i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6a0i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0i ProSAT]</span></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=6a0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0i OCA], [https://pdbe.org/6a0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a0i RCSB], [https://www.ebi.ac.uk/pdbsum/6a0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN]] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref>	+	[https://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Han~~, B W~~]]	+	[[Category: Han BW]]
-	[[Category: Park~~, J S]]~~	+	[[Category: Park JS]]
-	~~[[Category: Amidohydrolase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 06:46, 25 June 2020

OCA — Thu, 25 Jun 2020 06:46:26 GMT

←Older revision		Revision as of 06:46, 25 June 2020
Line 3:		Line 3:
	<StructureSection load='6a0i' size='340' side='right'caption='[[6a0i]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='6a0i' size='340' side='right'caption='[[6a0i]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6a0i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0I OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6A0I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6a0i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6A0I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6a0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0i OCA], [http://pdbe.org/6a0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a0i RCSB], [http://www.ebi.ac.uk/pdbsum/6a0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0i ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NTAN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6a0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0i OCA], [http://pdbe.org/6a0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a0i RCSB], [http://www.ebi.ac.uk/pdbsum/6a0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN]] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref>		[[http://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN]] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The N-degron pathway is a proteolytic system in which a single N-terminal amino acid acts as a determinant of protein degradation. Especially, degradation signaling of N-terminal asparagine (Nt-Asn) in eukaryotes is initiated from its deamidation by N-terminal asparagine amidohydrolase 1 (NTAN1) into aspartate. Here, we have elucidated structural principles of deamidation by human NTAN1. NTAN1 adopts the characteristic scaffold of CNF1/YfiH-like cysteine hydrolases that features an alpha-beta-beta sandwich structure and a catalytic triad comprising Cys, His, and Ser. In vitro deamidation assays using model peptide substrates with varying lengths and sequences showed that NTAN1 prefers hydrophobic residues at the second-position. The structures of NTAN1-peptide complexes further revealed that the recognition of Nt-Asn is sufficiently organized to produce high specificity, and the side chain of the second-position residue is accommodated in a hydrophobic pocket adjacent to the active site of NTAN1. Collectively, our structural and biochemical analyses of the substrate specificity of NTAN1 contribute to understanding the structural basis of all three amidases in the eukaryotic N-degron pathway.
		+
		+	Structural Analyses on the Deamidation of N-Terminal Asn in the Human N-Degron Pathway.,Park JS, Lee JY, Nguyen YTK, Kang NW, Oh EK, Jang DM, Kim HJ, Kim DD, Han BW Biomolecules. 2020 Jan 20;10(1). pii: biom10010163. doi: 10.3390/biom10010163. PMID:31968674<ref>PMID:31968674</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6a0i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Han, B W]]		[[Category: Han, B W]]

OCA at 15:01, 11 December 2019

OCA — Wed, 11 Dec 2019 15:01:50 GMT

←Older revision		Revision as of 15:01, 11 December 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6a0i is ~~ON HOLD until Dec 05 2020~~	+	==Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant==
-		+	<StructureSection load='6a0i' size='340' side='right'caption='[[6a0i]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~Authors~~: ~~Park~~, J.S., ~~Han~~, B.W.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6a0i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A0I FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~human protein~~ N-terminal asparagine ~~amidohydrolase~~ (~~NTAN1~~) ~~C75S mutant~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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=6a0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0i OCA], [http://pdbe.org/6a0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a0i RCSB], [http://www.ebi.ac.uk/pdbsum/6a0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0i ProSAT]</span></td></tr>
-	[[Category: Park, J.S]]	+	</table>
-	[[Category: ~~Han, B.W~~]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN]] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Han, B W]]
		+	[[Category: Park, J S]]
		+	[[Category: Amidohydrolase]]
		+	[[Category: Hydrolase]]

OCA at 03:47, 12 June 2019

OCA — Wed, 12 Jun 2019 03:47:39 GMT

←Older revision		Revision as of 03:47, 12 June 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6a0i is ON HOLD until ~~Paper Publication~~	+	The entry 6a0i is ON HOLD until Dec 05 2020

	Authors: Park, J.S., Han, B.W.		Authors: Park, J.S., Han, B.W.

OCA at 10:18, 16 January 2019

OCA — Wed, 16 Jan 2019 10:18:02 GMT

←Older revision		Revision as of 10:18, 16 January 2019
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	Authors: Park, J.S., Han, B.W.		Authors: Park, J.S., Han, B.W.

-	Description: ~~Protein~~ N-terminal asparagine amidohydrolase mutant ~~-C75S~~	+	Description: Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Park, J.S]]		[[Category: Park, J.S]]
	[[Category: Han, B.W]]		[[Category: Han, B.W]]

OCA at 04:46, 2 January 2019

OCA — Wed, 02 Jan 2019 04:46:09 GMT

←Older revision		Revision as of 04:46, 2 January 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6a0i is ON HOLD	+	The entry 6a0i is ON HOLD until Paper Publication

	Authors: Park, J.S., Han, B.W.		Authors: Park, J.S., Han, B.W.

OCA: Protected "6a0i" [edit=sysop:move=sysop]

OCA — Thu, 14 Jun 2018 05:27:31 GMT

Protected "6a0i" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:27, 14 June 2018

OCA: New page: '''Unreleased structure''' The entry 6a0i is ON HOLD Authors: Park, J.S., Han, B.W. Description: Protein N-terminal asparagine amidohydrolase mutant -C75S [[Category: Unreleased Struct...

OCA — Thu, 14 Jun 2018 05:27:30 GMT

New page: '''Unreleased structure''' The entry 6a0i is ON HOLD Authors: Park, J.S., Han, B.W. Description: Protein N-terminal asparagine amidohydrolase mutant -C75S [[Category: Unreleased Struct...

New page

'''Unreleased structure'''

The entry 6a0i is ON HOLD

Authors: Park, J.S., Han, B.W.

Description: Protein N-terminal asparagine amidohydrolase mutant -C75S
[[Category: Unreleased Structures]]
[[Category: Park, J.S]]
[[Category: Han, B.W]]