1yip - Revision history

OCA at 06:57, 23 August 2023

2023-08-23T06:57:27Z

← Older revision		Revision as of 06:57, 23 August 2023
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	<StructureSection load='1yip' size='340' side='right'caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1yip' size='340' side='right'caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1YIP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.2Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat~~">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1yi9\|1yi9]]~~, [[~~1phm~~\|~~1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw~~]]~~</div>~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~10116 Buffalo rat])</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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [https://pdbe.org/1yip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [https://www.ebi.ac.uk/pdbsum/1yip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3]~~ </~~span~~></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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [~~http~~://pdbe.org/1yip PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1yip PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.		[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	== 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: Buffalo rat]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Peptidylglycine monooxygenase~~]]		[[Category: Rattus norvegicus]]
	[[Category: Amzel~~, L M~~]]		[[Category: Amzel LM]]
	[[Category: Blackburn~~, N J~~]]		[[Category: Blackburn NJ]]
	[[Category: Eipper~~, B A~~]]		[[Category: Eipper BA]]
	[[Category: Mains~~, R E~~]]		[[Category: Mains RE]]
	[[Category: Prigge~~, S T~~]]		[[Category: Prigge ST]]
	[[Category: Siebert, X]]		[[Category: Siebert X]]
	~~[[Category: Ascorbate]]~~
	~~[[Category: Bioactive peptide activation]]~~
	~~[[Category: Copper]]~~
	~~[[Category: Monooxygenase]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 08:46, 20 January 2021

2021-01-20T08:46:30Z

← Older revision		Revision as of 08:46, 20 January 2021
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	==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==		==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==
	<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1yip' size='340' side='right'caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1YIP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	==See Also==		==See Also==
	*[[Monooxygenase\|Monooxygenase]]		*[[Monooxygenase 3D structures\|Monooxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
			[[Category: Large Structures]]
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Amzel, L M]]		[[Category: Amzel, L M]]

OCA at 06:50, 25 April 2018

2018-04-25T06:50:14Z

← Older revision		Revision as of 06:50, 25 April 2018
Line 1:		Line 1:

	==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==		==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==
	<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip 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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yi/1yip_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yi/1yip_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 1yip" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1yip" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Monooxygenase\|Monooxygenase]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Ascorbate]]		[[Category: Ascorbate]]
	[[Category: Bioactive peptide activation]]		[[Category: Bioactive peptide activation]]
			[[Category: Copper]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 15:14, 7 February 2016

2016-02-07T15:14:54Z

← Older revision		Revision as of 15:14, 7 February 2016
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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=1yip ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:42, 10 September 2015

2015-09-10T02:42:42Z

← Older revision		Revision as of 02:42, 10 September 2015
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	<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip 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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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 1yip" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Buffalo rat]]
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	~~[[Category: Rattus norvegicus]]~~
	[[Category: Amzel, L M]]		[[Category: Amzel, L M]]
	[[Category: Blackburn, N J]]		[[Category: Blackburn, N J]]

OCA at 16:12, 24 December 2014

2014-12-24T16:12:24Z

← Older revision		Revision as of 16:12, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip 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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Amzel, L M.]]		[[Category: Amzel, L M]]
	[[Category: Blackburn, N J.]]		[[Category: Blackburn, N J]]
	[[Category: Eipper, B A.]]		[[Category: Eipper, B A]]
	[[Category: Mains, R E.]]		[[Category: Mains, R E]]
	[[Category: Prigge, S T.]]		[[Category: Prigge, S T]]
	[[Category: Siebert, X.]]		[[Category: Siebert, X]]
	[[Category: Ascorbate]]		[[Category: Ascorbate]]
	[[Category: Bioactive peptide activation]]		[[Category: Bioactive peptide activation]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 21:30, 29 September 2014

2014-09-29T21:30:50Z

← Older revision		Revision as of 21:30, 29 September 2014
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	[[Image:~~1yip~~.~~png~~\|~~left~~\|~~200px~~]]		==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==
			<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yi9\|1yi9]], [[1phm\|1phm]], [[1opm\|1opm]], [[3phm\|3phm]], [[1sdw\|1sdw]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip 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/yi/1yip_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 ==
			Many bioactive peptides require amidation of their carboxy terminus to exhibit full biological activity. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first of the two steps of this reaction, is composed of two domains, each of which binds one copper atom (CuH and CuM). The CuM site includes Met(314) and two His residues as ligands. Mutation of Met(314) to Ile inactivates PHM, but has only a minimal effect on the EXAFS spectrum of the oxidized enzyme, implying that it contributes only marginally to stabilization of the CuM site. To characterize the role of Met(314) as a CuM ligand, we determined the structure of the Met(314)Ile-PHM mutant. Since the mutant protein failed to crystallize in the conditions of the original wild-type protein, this structure determination required finding a new crystal form. The Met(314)Ile-PHM mutant structure confirms that the mutation does not abolish CuM binding to the enzyme, but causes other structural perturbations that affect the overall stability of the enzyme and the integrity of the CuH site. To eliminate possible effects of crystal contacts, we redetermined the structure of wt-PHM in the Met(314)Ile-PHM crystal form and showed that it does not differ from the structure of wild-type (wt)-PHM in the original crystals. Met(314)Ile-PHM was also shown to be less stable than wt-PHM by differential scanning calorimetry. Both structural and calorimetric studies point to a structural role for the CuM site, in addition to its established catalytic role.

	~~{{STRUCTURE_1yip\| PDB=1yip \| SCENE= }}~~		The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.,Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:16100265<ref>PMID:16100265</ref>

	~~===Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_16100265}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[1yip]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:016100265<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]

OCA: Protected "1yip" [edit=sysop:move=sysop]

2013-01-05T17:30:13Z

Protected "1yip" [edit=sysop:move=sysop]

← Older revision	Revision as of 17:30, 5 January 2013
(No difference)

OCA at 17:30, 5 January 2013

2013-01-05T17:30:11Z

← Older revision		Revision as of 17:30, 5 January 2013
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	~~{{Seed}}~~
	[[Image:1yip.png\|left\|200px]]		[[Image:1yip.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_1yip", 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_1yip\| PDB=1yip \| SCENE= }}		{{STRUCTURE_1yip\| PDB=1yip \| SCENE= }}

	===Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form===		===Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_16100265}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 16100265 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_16100265}}		{{ABSTRACT_PUBMED_16100265}}

	==About this Structure==		==About this Structure==
	~~1YIP~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA].		[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~16100265~~</ref><references group="xtra"/>		<ref group="xtra">PMID:016100265</ref><references group="xtra"/>
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 34:		Line 22:
	[[Category: Ascorbate]]		[[Category: Ascorbate]]
	[[Category: Bioactive peptide activation]]		[[Category: Bioactive peptide activation]]
	~~[[Category: Copper]]~~
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:43:00 2009''~~

OCA at 12:43, 16 February 2009

2009-02-16T12:43:02Z

← Older revision		Revision as of 12:43, 16 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	1YIP is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA].		1YIP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA].

	==Reference==		==Reference==
	The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role., Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM, Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16100265 16100265]~~		<ref group="xtra">PMID:16100265</ref><references group="xtra"/>
	[[Category: Peptidylglycine monooxygenase]]		[[Category: Peptidylglycine monooxygenase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	~~[[Category: Single protein]]~~
	[[Category: Amzel, L M.]]		[[Category: Amzel, L M.]]
	[[Category: Blackburn, N J.]]		[[Category: Blackburn, N J.]]
Line 39:		Line 38:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Jul 27 17~~:25:~~28 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:43:00 2009''