2zed - Revision history

OCA at 13:33, 1 November 2023

2023-11-01T13:33:36Z

← Older revision		Revision as of 13:33, 1 November 2023
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	<StructureSection load='2zed' size='340' side='right'caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2zed' size='340' side='right'caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZED FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zed]] 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=2ZED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZED FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</div>~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>QPCT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5]~~ </~~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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [https://pdbe.org/2zed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [https://www.ebi.ac.uk/pdbsum/2zed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zed 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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [https://pdbe.org/2zed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [https://www.ebi.ac.uk/pdbsum/2zed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zed ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>		[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Glutaminyl-peptide cyclotransferase]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Chang~~, E C~~]]		[[Category: Chang EC]]
	[[Category: Chou~~, T L~~]]		[[Category: Chou TL]]
	[[Category: Huang~~, K F~~]]		[[Category: Huang KF]]
	[[Category: Wang~~, A H~~]]		[[Category: Wang AH]]
	[[Category: Wang~~, Y R]]~~		[[Category: Wang YR]]
	~~[[Category: Acyltransferase]]~~
	~~[[Category: Glutaminyl cyclase]]~~
	~~[[Category: Glycoprotein]]~~
	~~[[Category: Hydrogen bond network]]~~
	~~[[Category: Metal-binding]]~~
	~~[[Category: Proton transfer]]~~
	~~[[Category: Pyroglutamate]]~~
	~~[[Category: Site-directed mutagenesis]]~~
	~~[[Category: Transferase~~]]

OCA at 07:15, 10 November 2021

2021-11-10T07:15:02Z

← Older revision		Revision as of 07:15, 10 November 2021
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	==Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution==		==Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution==
	<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2zed' size='340' side='right'caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zed]] 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=2ZED OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ZED FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZED FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [~~http~~://pdbe.org/2zed PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2zed PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2zed 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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [https://pdbe.org/2zed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [https://www.ebi.ac.uk/pdbsum/2zed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zed ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>		[[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/2zed_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/2zed_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 2zed" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2zed" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Glutaminyl cyclase\|Glutaminyl cyclase]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Chang, E C]]		[[Category: Chang, E C]]
	[[Category: Chou, T L]]		[[Category: Chou, T L]]

OCA at 12:19, 12 October 2017

2017-10-12T12:19:56Z

← Older revision		Revision as of 12:19, 12 October 2017
Line 1:		Line 1:

	==Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution==		==Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution==
	<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://pdbe.org/2zed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://pdbe.org/2zed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zed ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 2zed" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2zed" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Glutaminyl cyclase\|Glutaminyl cyclase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:04, 9 February 2016

2016-02-09T02:04:48Z

← Older revision		Revision as of 02:04, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZED FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zed]] 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=2ZED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZED FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://pdbe.org/2zed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zed ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2zed" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	</StructureSection>		</StructureSection>
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Chang, E C]]		[[Category: Chang, E C]]
	[[Category: Chou, T L]]		[[Category: Chou, T L]]

OCA at 03:40, 25 December 2014

2014-12-25T03:40:23Z

← Older revision		Revision as of 03:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZED FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZED FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></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=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chang, E C.]]		[[Category: Chang, E C]]
	[[Category: Chou, T L.]]		[[Category: Chou, T L]]
	[[Category: Huang, K F.]]		[[Category: Huang, K F]]
	[[Category: Wang, A H.]]		[[Category: Wang, A H]]
	[[Category: Wang, Y R.]]		[[Category: Wang, Y R]]
	[[Category: Acyltransferase]]		[[Category: Acyltransferase]]
	[[Category: Glutaminyl cyclase]]		[[Category: Glutaminyl cyclase]]

OCA at 04:45, 2 October 2014

2014-10-02T04:45:21Z

← Older revision		Revision as of 04:45, 2 October 2014
Line 1:		Line 1:
	[[Image:~~2zed~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution==
			<StructureSection load='2zed' size='340' side='right' caption='[[2zed]], [[Resolution\|resolution]] 1.70Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZED FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2afm\|2afm]], [[2zee\|2zee]], [[2zef\|2zef]], [[2zeg\|2zeg]], [[2zeh\|2zeh]], [[2zel\|2zel]], [[2zem\|2zem]], [[2zen\|2zen]], [[2zeo\|2zeo]], [[2zep\|2zep]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zed OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zed RCSB], [http://www.ebi.ac.uk/pdbsum/2zed PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/2zed_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			QCs (glutaminyl cyclases; glutaminyl-peptide cyclotransferases, EC 2.3.2.5) catalyse N-terminal pyroglutamate formation in numerous bioactive peptides and proteins. The enzymes were reported to be involved in several pathological conditions such as amyloidotic disease, osteoporosis, rheumatoid arthritis and melanoma. The crystal structure of human QC revealed an unusual H-bond (hydrogen-bond) network in the active site, formed by several highly conserved residues (Ser(160), Glu(201), Asp(248), Asp(305) and His(319)), within which Glu(201) and Asp(248) were found to bind to substrate. In the present study we combined steady-state enzyme kinetic and X-ray structural analyses of 11 single-mutation human QCs to investigate the roles of the H-bond network in catalysis. Our results showed that disrupting one or both of the central H-bonds, i.e., Glu(201)...Asp(305) and Asp(248)...Asp(305), reduced the steady-state catalysis dramatically. The roles of these two COOH...COOH bonds on catalysis could be partly replaced by COOH...water bonds, but not by COOH...CONH(2) bonds, reminiscent of the low-barrier Asp...Asp H-bond in the active site of pepsin-like aspartic peptidases. Mutations on Asp(305), a residue located at the centre of the H-bond network, raised the K(m) value of the enzyme by 4.4-19-fold, but decreased the k(cat) value by 79-2842-fold, indicating that Asp(305) primarily plays a catalytic role. In addition, results from mutational studies on Ser(160) and His(319) suggest that these two residues might help to stabilize the conformations of Asp(248) and Asp(305) respectively. These data allow us to propose an essential proton transfer between Glu(201), Asp(305) and Asp(248) during the catalysis by animal QCs.

	~~{{STRUCTURE_2zed\| PDB=2zed \| SCENE= }}~~		A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis.,Huang KF, Wang YR, Chang EC, Chou TL, Wang AH Biochem J. 2008 Apr 1;411(1):181-90. PMID:18072935<ref>PMID:18072935</ref>

	~~===Crystal structure~~ of the ~~human glutaminyl cyclase mutant S160A at 1~~.~~7 angstrom resolution===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_18072935}}~~		==See Also==
			*[[Glutaminyl cyclase\|Glutaminyl cyclase]]
	==~~About this Structure~~==		== References ==
	[[~~2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens~~]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:018072935<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "2zed" [edit=sysop:move=sysop]

2013-01-07T19:10:46Z

Protected "2zed" [edit=sysop:move=sysop]

← Older revision	Revision as of 19:10, 7 January 2013
(No difference)

OCA at 19:10, 7 January 2013

2013-01-07T19:10:44Z

← Older revision		Revision as of 19:10, 7 January 2013
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	~~{{Seed}}~~
	[[Image:2zed.png\|left\|200px]]		[[Image:2zed.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2zed", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2zed\| PDB=2zed \| SCENE= }}		{{STRUCTURE_2zed\| PDB=2zed \| SCENE= }}

	===Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution===		===Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_18072935}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 18072935 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_18072935}}		{{ABSTRACT_PUBMED_18072935}}

	==About this Structure==		==About this Structure==
	~~2ZED~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA].		[[2zed]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~18072935~~</ref><references group="xtra"/>		<ref group="xtra">PMID:018072935</ref><references group="xtra"/>
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 36:		Line 24:
	[[Category: Hydrogen bond network]]		[[Category: Hydrogen bond network]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	~~[[Category: Polymorphism]]~~
	[[Category: Proton transfer]]		[[Category: Proton transfer]]
	[[Category: Pyroglutamate]]		[[Category: Pyroglutamate]]
	[[Category: Site-directed mutagenesis]]		[[Category: Site-directed mutagenesis]]
	[[Category: Transferase]]		[[Category: Transferase]]
	~~[[Category: Zinc]]~~

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:35:04 2009''~~

OCA at 03:35, 17 February 2009

2009-02-17T03:35:07Z

← Older revision		Revision as of 03:35, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2ZED is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA].		2ZED is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZED OCA].

	==Reference==		==Reference==
	~~A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis., Huang KF, Wang YR, Chang EC, Chou TL, Wang AH, Biochem J. 2008 Apr 1;411(1):181-90.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18072935 18072935]~~		<ref group="xtra">PMID:18072935</ref><references group="xtra"/>
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	~~[[Category: Single protein]]~~
	[[Category: Chang, E C.]]		[[Category: Chang, E C.]]
	[[Category: Chou, T L.]]		[[Category: Chou, T L.]]
Line 44:		Line 43:
	[[Category: Zinc]]		[[Category: Zinc]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 08~~:57:~~55 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:35:04 2009''

OCA at 05:57, 28 July 2008

2008-07-28T05:57:57Z

← Older revision		Revision as of 05:57, 28 July 2008
Line 1:		Line 1:
	[[Image:2zed.~~jpg~~\|left\|200px]]		{{Seed}}
			[[Image:2zed.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2zed\| PDB=2zed \| SCENE= }}		{{STRUCTURE_2zed\| PDB=2zed \| SCENE= }}

	~~'''~~Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution~~'''~~		===Crystal structure of the human glutaminyl cyclase mutant S160A at 1.7 angstrom resolution===


	~~==Overview==~~		<!--
	~~QCs (glutaminyl cyclases; glutaminyl~~-~~peptide cyclotransferases, EC 2.3.2.5) catalyse N~~-~~terminal pyroglutamate formation in numerous bioactive peptides and proteins.~~ The ~~enzymes were reported to be involved in several pathological conditions such as amyloidotic disease~~, osteoporosis, rheumatoid arthritis and melanoma. The crystal structure of human QC revealed an unusual H-bond (hydrogen-bond) network in the active site, formed by several highly conserved residues (Ser(160), Glu(201), Asp(248), Asp(305) and His(319)), ~~within which Glu(201) and Asp(248) were found to bind to substrate. In~~ the ~~present study we combined steady-state enzyme kinetic and X-ray structural analyses of 11 single-mutation human QCs~~ to ~~investigate~~ the ~~roles of the H-bond network in catalysis. Our results showed that disrupting one or both of the central H-bonds, i.e., Glu~~(~~201)...Asp(305) and Asp(248)...Asp(305), reduced the steady-state catalysis dramatically. The roles of these two COOH...COOH bonds~~ on ~~catalysis could be partly replaced by COOH..~~.~~water bonds, but not by COOH~~.~~..CONH(2~~) ~~bonds~~, ~~reminiscent of~~ the ~~low-barrier Asp~~.~~..Asp H~~-~~bond in the active site of pepsin~~-like aspartic peptidases. Mutations on Asp(305), a residue located at the centre of the H-bond network, raised the K(m) value of the enzyme by 4.4-19-fold, but decreased the k(cat) value by 79-2842-fold, indicating that Asp(305) primarily plays a catalytic role. In addition, results from mutational studies on Ser(160) and His(319) suggest that these two residues might help to stabilize the conformations of Asp(248) and Asp(305) respectively. These data allow us to propose an essential proton transfer between Glu(201), Asp(305) and Asp(248) during the catalysis by animal QCs.		The line below this paragraph, {{ABSTRACT_PUBMED_18072935}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 18072935 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_18072935}}

	==About this Structure==		==About this Structure==
Line 39:		Line 43:
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Zinc]]		[[Category: Zinc]]
	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Apr 24 09~~:45:19 2008''
			''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:57:55 2008''