2anp - Revision history

OCA at 07:26, 23 August 2023

2023-08-23T07:26:51Z

←Older revision		Revision as of 07:26, 23 August 2023
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	<StructureSection load='2anp' size='340' side='right'caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2anp' size='340' side='right'caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10]~~ </~~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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [https://pdbe.org/2anp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [https://www.ebi.ac.uk/pdbsum/2anp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2anp 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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [https://pdbe.org/2anp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [https://www.ebi.ac.uk/pdbsum/2anp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2anp ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/AMPX_VIBPR AMPX_VIBPR]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Aeromonas proteolytica merkel et al. 1964]]
-	[[Category: Bacterial leucyl aminopeptidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bzymek~~, K P~~]]	+	[[Category: Vibrio proteolyticus]]
-	[[Category: Holz~~, R C~~]]	+	[[Category: Bzymek KP]]
-	[[Category: Moulin, A]]	+	[[Category: Holz RC]]
-	[[Category: Petsko~~, G A~~]]	+	[[Category: Moulin A]]
-	[[Category: Ringe, D]]	+	[[Category: Petsko GA]]
-	[[Category: Swierczek~~, S I]]~~	+	[[Category: Ringe D]]
-	~~[[Category: Aminopeptidase]]~~	+	[[Category: Swierczek SI]]
-	~~[[Category: Bi-metallic]]~~	+
-	~~[[Category: Epr]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Spectroscopy]]~~	+
-	~~[[Category: Zinc~~]]	+

OCA at 06:37, 6 October 2021

2021-10-06T06:37:00Z

←Older revision		Revision as of 06:37, 6 October 2021
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	<StructureSection load='2anp' size='340' side='right'caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2anp' size='340' side='right'caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ANP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=NA:SODIUM+ION'>NA</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">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [~~http~~://pdbe.org/2anp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2anp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2anp 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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [https://pdbe.org/2anp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [https://www.ebi.ac.uk/pdbsum/2anp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2anp ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 19:44, 11 December 2019

2019-12-11T19:44:17Z

←Older revision		Revision as of 19:44, 11 December 2019
Line 1:		Line 1:

	==Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.==		==Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.==
-	<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='2anp' size='340' side='right'caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 2anp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2anp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	[[Category: Aeromonas proteolytica merkel et al. 1964]]		[[Category: Aeromonas proteolytica merkel et al. 1964]]
	[[Category: Bacterial leucyl aminopeptidase]]		[[Category: Bacterial leucyl aminopeptidase]]
		+	[[Category: Large Structures]]
	[[Category: Bzymek, K P]]		[[Category: Bzymek, K P]]
	[[Category: Holz, R C]]		[[Category: Holz, R C]]

OCA at 06:36, 31 January 2018

2018-01-31T06:36:37Z

←Older revision		Revision as of 06:36, 31 January 2018
Line 1:		Line 1:
		+
	==Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.==		==Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.==
	<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://pdbe.org/2anp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp 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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://pdbe.org/2anp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2anp ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/2anp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/2anp_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>
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 2anp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2anp" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
	== References ==		== References ==
	<references/>		<references/>
Line 47:		Line 45:
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Spectroscopy]]		[[Category: Spectroscopy]]
		+	[[Category: Zinc]]

OCA at 22:57, 9 February 2016

2016-02-09T22:57:26Z

←Older revision		Revision as of 22:57, 9 February 2016
Line 16:		Line 16:
	<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=2anp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:53, 11 September 2015

2015-09-11T02:53:18Z

←Older revision		Revision as of 02:53, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Vibrio_proteolyticus Vibrio proteolyticus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=NA:SODIUM+ION'>NA</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">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp 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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://pdbe.org/2anp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 26:
	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 2anp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aeromonas proteolytica merkel et al. 1964]]
	[[Category: Bacterial leucyl aminopeptidase]]		[[Category: Bacterial leucyl aminopeptidase]]
-	[[Category: Vibrio proteolyticus]]
	[[Category: Bzymek, K P]]		[[Category: Bzymek, K P]]
	[[Category: Holz, R C]]		[[Category: Holz, R C]]

OCA at 10:41, 8 January 2015

2015-01-08T10:41:09Z

←Older revision		Revision as of 10:41, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp 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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Bacterial leucyl aminopeptidase]]		[[Category: Bacterial leucyl aminopeptidase]]
	[[Category: Vibrio proteolyticus]]		[[Category: Vibrio proteolyticus]]
-	[[Category: Bzymek, K P.]]	+	[[Category: Bzymek, K P]]
-	[[Category: Holz, R C.]]	+	[[Category: Holz, R C]]
-	[[Category: Moulin, A.]]	+	[[Category: Moulin, A]]
-	[[Category: Petsko, G A.]]	+	[[Category: Petsko, G A]]
-	[[Category: Ringe, D.]]	+	[[Category: Ringe, D]]
-	[[Category: Swierczek, S I.]]	+	[[Category: Swierczek, S I]]
	[[Category: Aminopeptidase]]		[[Category: Aminopeptidase]]
	[[Category: Bi-metallic]]		[[Category: Bi-metallic]]

OCA at 05:23, 29 September 2014

2014-09-29T05:23:49Z

←Older revision		Revision as of 05:23, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2anp.~~png~~\|~~left~~\|200px]]	+	==Functional Glutamate 151 to Histidine mutant of the aminopeptidase from Aeromonas Proteolytica.==
		+	<StructureSection load='2anp' size='340' side='right' caption='[[2anp]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1amp\|1amp]], [[1lok\|1lok]], [[1cp6\|1cp6]], [[1txr\|1txr]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </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=2anp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2anp RCSB], [http://www.ebi.ac.uk/pdbsum/2anp 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/an/2anp_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 ==
		+	Glutamate151 (E151) has been shown to be catalytically essential for the aminopeptidase from Vibrio proteolyticus (AAP). E151 acts as the general acid/base during the catalytic mechanism of peptide hydrolysis. However, a glutamate residue is not the only residue capable of functioning as a general acid/base during catalysis for dinuclear metallohydrolases. Recent crystallographic characterization of the D-aminopeptidase from Bacillus subtilis (DppA) revealed a histidine residue that resides in an identical position to E151 in AAP. Because the active-site ligands for DppA and AAP are identical, AAP has been used as a model enzyme to understand the mechanistic role of H115 in DppA. Substitution of E151 with histidine resulted in an active AAP enzyme exhibiting a kcat value of 2.0 min(-1), which is over 2000 times slower than r AAP (4380 min(-1)). ITC experiments revealed that ZnII binds 330 and 3 times more weakly to E151H-AAP compared to r-AAP. UV-vis and EPR spectra of CoII-loaded E151H-AAP indicated that the first metal ion resides in a hexacoordinate/pentacoordinate equilibrium environment, whereas the second metal ion is six-coordinate. pH dependence of the kinetic parameters kcat and K(m) for the hydrolysis of L-leucine p-nitroanilide (L-pNA) revealed a change in an ionization constant in the enzyme-substrate complex from 5.3 in r-AAP to 6.4 in E151H-AAP, consistent with E151 in AAP being the active-site general acid/base. Proton inventory studies at pH 8.50 indicate the transfer of one proton in the rate-limiting step of the reaction. Moreover, the X-ray crystal structure of [ZnZn(E151H-AAP)] has been solved to 1.9 A resolution, and alteration of E151 to histidine does not introduce any major conformational changes to the overall protein structure or the dinuclear ZnII active site. Therefore, a histidine residue can function as the general acid/base in hydrolysis reactions of peptides and, through analogy of the role of E151 in AAP, H115 in DppA likely shuttles a proton to the leaving group of the substrate.

-	~~{{STRUCTURE_2anp\| PDB=2anp \| SCENE= }}~~	+	Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica.,Bzymek KP, Moulin A, Swierczek SI, Ringe D, Petsko GA, Bennett B, Holz RC Biochemistry. 2005 Sep 13;44(36):12030-40. PMID:16142900<ref>PMID:16142900</ref>

-	~~===Functional Glutamate 151 to Histidine mutant~~ of the ~~aminopeptidase from Aeromonas Proteolytica~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16142900}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2anp]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA].~~	+

	==See Also==		==See Also==
	*[[Aminopeptidase\|Aminopeptidase]]		*[[Aminopeptidase\|Aminopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016142900<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bacterial leucyl aminopeptidase]]		[[Category: Bacterial leucyl aminopeptidase]]
	[[Category: Vibrio proteolyticus]]		[[Category: Vibrio proteolyticus]]

OCA at 15:26, 20 October 2012

2012-10-20T15:26:15Z

←Older revision		Revision as of 15:26, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2anp]] is a 1 chain structure ~~of [[Aminopeptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA].	+	[[2anp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANP OCA].

	==See Also==		==See Also==

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

2012-07-26T18:22:32Z

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

←Older revision

Revision as of 18:22, 26 July 2012