2zee - Revision history

OCA at 13:33, 1 November 2023

OCA — Wed, 01 Nov 2023 13:33:52 GMT

←Older revision		Revision as of 13:33, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='2zee' size='340' side='right'caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2zee' size='340' side='right'caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZEE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZEE 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]] 1.99Å</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]], [[2zed\|2zed]], [[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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [https://pdbe.org/2zee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [https://www.ebi.ac.uk/pdbsum/2zee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zee 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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [https://pdbe.org/2zee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [https://www.ebi.ac.uk/pdbsum/2zee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zee 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: Glutaminyl cyclase]]~~	+
-	~~[[Category: Hydrogen bond network]]~~	+
-	~~[[Category: Proton transfer]]~~	+
-	~~[[Category: Pyroglutamate]]~~	+
-	~~[[Category: Site-directed mutagenesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:15, 10 November 2021

OCA — Wed, 10 Nov 2021 07:15:04 GMT

←Older revision		Revision as of 07:15, 10 November 2021
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	==Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution==		==Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution==
-	<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>	+	<StructureSection load='2zee' size='340' side='right'caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ZEE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZEE 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]], [[2zed\|2zed]], [[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]], [[2zed\|2zed]], [[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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [~~http~~://pdbe.org/2zee PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2zee PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2zee 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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [https://pdbe.org/2zee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [https://www.ebi.ac.uk/pdbsum/2zee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zee 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]]
Line 40:		Line 40:
	[[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 07:33, 18 October 2018

OCA — Thu, 18 Oct 2018 07:33:58 GMT

←Older revision		Revision as of 07:33, 18 October 2018
Line 1:		Line 1:
		+
	==Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution==		==Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution==
	<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>
Line 7:		Line 8:
	<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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://pdbe.org/2zee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee 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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://pdbe.org/2zee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zee ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/2zee_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/2zee_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>

OCA at 07:50, 7 February 2016

OCA — Sun, 07 Feb 2016 07:50:13 GMT

←Older revision		Revision as of 07:50, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEE 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]], [[2zed\|2zed]], [[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]], [[2zed\|2zed]], [[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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee 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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://pdbe.org/2zee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	<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=2zee ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 2zee" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	</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 09:06, 24 December 2014

OCA — Wed, 24 Dec 2014 09:06:18 GMT

←Older revision		Revision as of 09:06, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEE 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]], [[2zed\|2zed]], [[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]], [[2zed\|2zed]], [[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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee 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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee 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: Glutaminyl cyclase]]		[[Category: Glutaminyl cyclase]]
	[[Category: Hydrogen bond network]]		[[Category: Hydrogen bond network]]

OCA at 05:12, 2 October 2014

OCA — Thu, 02 Oct 2014 05:12:53 GMT

←Older revision		Revision as of 05:12, 2 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2zee.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution==
		+	<StructureSection load='2zee' size='340' side='right' caption='[[2zee]], [[Resolution\|resolution]] 1.99Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2zee]] 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=2ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZEE 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]], [[2zed\|2zed]], [[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=2zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zee RCSB], [http://www.ebi.ac.uk/pdbsum/2zee 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/2zee_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_2zee\| PDB=2zee \| 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 S160G at 1~~.~~99 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 ==
-	[[~~2zee~~]] 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=2ZEE 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 "2zee" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 19:46:46 GMT

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

←Older revision

Revision as of 19:46, 7 January 2013

OCA at 19:46, 7 January 2013

OCA — Mon, 07 Jan 2013 19:46:43 GMT

←Older revision		Revision as of 19:46, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2zee.png\|left\|200px]]		[[Image:2zee.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2zee", 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_2zee\| PDB=2zee \| SCENE= }}		{{STRUCTURE_2zee\| PDB=2zee \| SCENE= }}

	===Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution===		===Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 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==
-	~~2ZEE~~ 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=2ZEE OCA].	+	[[2zee]] 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=2ZEE 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 37:		Line 25:
	[[Category: Site-directed mutagenesis]]		[[Category: Site-directed mutagenesis]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:22:54 2009''

OCA at 10:22, 16 February 2009

OCA — Mon, 16 Feb 2009 10:22:56 GMT

←Older revision		Revision as of 10:22, 16 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2ZEE 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=2ZEE OCA].	+	2ZEE 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=2ZEE 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 39:		Line 38:
	[[Category: Transferase]]		[[Category: Transferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Jul 27 14~~:34:~~43 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:22:54 2009''

OCA at 11:34, 27 July 2008

OCA — Sun, 27 Jul 2008 11:34:44 GMT

←Older revision		Revision as of 11:34, 27 July 2008
Line 1:		Line 1:
-	[[Image:2zee.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2zee.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2zee\| PDB=2zee \| SCENE= }}		{{STRUCTURE_2zee\| PDB=2zee \| SCENE= }}

-	~~'''~~Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 angstrom resolution~~'''~~	+	===Crystal structure of the human glutaminyl cyclase mutant S160G at 1.99 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 34:		Line 38:
	[[Category: Site-directed mutagenesis]]		[[Category: Site-directed mutagenesis]]
	[[Category: Transferase]]		[[Category: Transferase]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Apr 24 09~~:45:23 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:34:43 2008''