3h8e - Revision history

OCA at 09:58, 21 February 2024

OCA — Wed, 21 Feb 2024 09:58:34 GMT

←Older revision		Revision as of 09:58, 21 February 2024
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	<StructureSection load='3h8e' size='340' side='right'caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='3h8e' size='340' side='right'caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8E FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</div></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]] 2.75Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">pepA ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [https://pdbe.org/3h8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [https://www.ebi.ac.uk/pdbsum/3h8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8e 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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [https://pdbe.org/3h8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [https://www.ebi.ac.uk/pdbsum/3h8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AMPA_PSEPU AMPA_PSEPU]] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).	+	[https://www.uniprot.org/uniprot/AMPA_PSEPU AMPA_PSEPU] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3h8e 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=3h8e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The zinc-dependent leucine aminopeptidase from Pseudomonas putida (ppLAP) is an important enzyme for the industrial production of enantiomerically pure amino acids. To provide a better understanding of its structure-function relationships, the enzyme was studied by X-ray crystallography. Crystal structures of native ppLAP at pH 9.5 and pH 5.2, and in complex with the inhibitor bestatin, show that the overall folding and hexameric organization of ppLAP are very similar to those of the closely related di-zinc leucine aminopeptidases (LAPs) from bovine lens and Escherichia coli. At pH 9.5, the active site contains two metal ions, one identified as Mn(2+) or Zn(2+) (site 1), and the other as Zn(2+) (site 2). By using a metal-dependent activity assay it was shown that site 1 in heterologously expressed ppLAP is occupied mainly by Mn(2+). Moreover, it was shown that Mn(2+) has a significant activation effect when bound to site 1 of ppLAP. At pH 5.2, the active site of ppLAP is highly disordered and the two metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267, explaining why ppLAP is inactive at low pH. A structural comparison of the ppLAP-bestatin complex with inhibitor-bound complexes of bovine lens LAP, along with substrate modelling, gave clear and new insights into its substrate specificity and high level of enantioselectivity.
-
-	Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity.,Kale A, Pijning T, Sonke T, Dijkstra BW, Thunnissen AM J Mol Biol. 2010 May 21;398(5):703-14. Epub 2010 Mar 30. PMID:20359484<ref>PMID:20359484</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3h8e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]		*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Leucyl aminopeptidase~~]]	+	[[Category: Pseudomonas putida]]
-	[[Category: Dijkstra~~, B W~~]]	+	[[Category: Dijkstra BW]]
-	[[Category: Kale, A]]	+	[[Category: Kale A]]
-	[[Category: Sonke, T]]	+	[[Category: Sonke T]]
-	[[Category: Thunnissen~~, A M.W H]]~~	+	[[Category: Thunnissen AMWH]]
-	~~[[Category: Aminopeptidase]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Manganese]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Protease~~]]	+

OCA at 08:05, 16 March 2022

OCA — Wed, 16 Mar 2022 08:05:59 GMT

←Older revision		Revision as of 08:05, 16 March 2022
Line 1:		Line 1:

	==Low pH native structure of leucine aminopeptidase from Pseudomonas putida==		==Low pH native structure of leucine aminopeptidase from Pseudomonas putida==
-	<StructureSection load='3h8e' size='340' side='right' caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>	+	<StructureSection load='3h8e' size='340' side='right'caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3H8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H8E FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [~~http~~://pdbe.org/3h8e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3h8e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8e 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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [https://pdbe.org/3h8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [https://www.ebi.ac.uk/pdbsum/3h8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AMPA_PSEPU AMPA_PSEPU]] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).	+	[[https://www.uniprot.org/uniprot/AMPA_PSEPU AMPA_PSEPU]] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3h8e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3h8e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
		+	[[Category: Large Structures]]
	[[Category: Leucyl aminopeptidase]]		[[Category: Leucyl aminopeptidase]]
	[[Category: Dijkstra, B W]]		[[Category: Dijkstra, B W]]

OCA at 19:19, 24 January 2018

OCA — Wed, 24 Jan 2018 19:19:33 GMT

←Older revision		Revision as of 19:19, 24 January 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/3h8e_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/3h8e_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3h8e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3h8e" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Thunnissen, A M.W H]]		[[Category: Thunnissen, A M.W H]]
	[[Category: Aminopeptidase]]		[[Category: Aminopeptidase]]
		+	[[Category: Cytoplasm]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Manganese]]		[[Category: Manganese]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Protease]]		[[Category: Protease]]

OCA at 16:23, 5 August 2016

OCA — Fri, 05 Aug 2016 16:23:45 GMT

←Older revision		Revision as of 16:23, 5 August 2016
Line 1:		Line 1:
		+
	==Low pH native structure of leucine aminopeptidase from Pseudomonas putida==		==Low pH native structure of leucine aminopeptidase from Pseudomonas putida==
	<StructureSection load='3h8e' size='340' side='right' caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='3h8e' size='340' side='right' caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pseudomonas_putida Pseudomonas putida~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H8E FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 ~~Pseudomonas putida~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [http://www.ebi.ac.uk/pdbsum/3h8e 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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [http://pdbe.org/3h8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [http://www.ebi.ac.uk/pdbsum/3h8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		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=3h8e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		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 3h8e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Leucyl aminopeptidase]]		[[Category: Leucyl aminopeptidase]]
-	[[Category: Pseudomonas putida]]
	[[Category: Dijkstra, B W]]		[[Category: Dijkstra, B W]]
	[[Category: Kale, A]]		[[Category: Kale, A]]

OCA at 20:14, 25 December 2014

OCA — Thu, 25 Dec 2014 20:14:14 GMT

←Older revision		Revision as of 20:14, 25 December 2014
Line 8:		Line 8:
	<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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [http://www.ebi.ac.uk/pdbsum/3h8e 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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [http://www.ebi.ac.uk/pdbsum/3h8e PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPA_PSEPU AMPA_PSEPU]] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:19, 8 December 2014

OCA — Mon, 08 Dec 2014 09:19:18 GMT

←Older revision		Revision as of 09:19, 8 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3h8e.~~png~~\|~~left~~\|200px]]	+	==Low pH native structure of leucine aminopeptidase from Pseudomonas putida==
		+	<StructureSection load='3h8e' size='340' side='right' caption='[[3h8e]], [[Resolution\|resolution]] 2.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3h8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H8E FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1gyt\|1gyt]], [[1bll\|1bll]], [[3h8f\|3h8f]], [[3h8g\|3h8g]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </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=3h8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h8e RCSB], [http://www.ebi.ac.uk/pdbsum/3h8e 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/h8/3h8e_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 ==
		+	The zinc-dependent leucine aminopeptidase from Pseudomonas putida (ppLAP) is an important enzyme for the industrial production of enantiomerically pure amino acids. To provide a better understanding of its structure-function relationships, the enzyme was studied by X-ray crystallography. Crystal structures of native ppLAP at pH 9.5 and pH 5.2, and in complex with the inhibitor bestatin, show that the overall folding and hexameric organization of ppLAP are very similar to those of the closely related di-zinc leucine aminopeptidases (LAPs) from bovine lens and Escherichia coli. At pH 9.5, the active site contains two metal ions, one identified as Mn(2+) or Zn(2+) (site 1), and the other as Zn(2+) (site 2). By using a metal-dependent activity assay it was shown that site 1 in heterologously expressed ppLAP is occupied mainly by Mn(2+). Moreover, it was shown that Mn(2+) has a significant activation effect when bound to site 1 of ppLAP. At pH 5.2, the active site of ppLAP is highly disordered and the two metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267, explaining why ppLAP is inactive at low pH. A structural comparison of the ppLAP-bestatin complex with inhibitor-bound complexes of bovine lens LAP, along with substrate modelling, gave clear and new insights into its substrate specificity and high level of enantioselectivity.

-	~~{{STRUCTURE_3h8e\| PDB=3h8e \| SCENE= }}~~	+	Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity.,Kale A, Pijning T, Sonke T, Dijkstra BW, Thunnissen AM J Mol Biol. 2010 May 21;398(5):703-14. Epub 2010 Mar 30. PMID:20359484<ref>PMID:20359484</ref>

-	~~===Low pH native structure~~ of ~~leucine aminopeptidase from Pseudomonas putida===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20359484}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3h8e]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Pseudomonas_putida Pseudomonas putida]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].~~	+

	==See Also==		==See Also==
	*[[Aminopeptidase\|Aminopeptidase]]		*[[Aminopeptidase\|Aminopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020359484<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Leucyl aminopeptidase]]		[[Category: Leucyl aminopeptidase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
-	[[Category: Dijkstra, B W.]]	+	[[Category: Dijkstra, B W]]
-	[[Category: Kale, A.]]	+	[[Category: Kale, A]]
-	[[Category: Sonke, T.]]	+	[[Category: Sonke, T]]
	[[Category: Thunnissen, A M.W H]]		[[Category: Thunnissen, A M.W H]]
	[[Category: Aminopeptidase]]		[[Category: Aminopeptidase]]

OCA at 20:59, 20 October 2012

OCA — Sat, 20 Oct 2012 20:59:20 GMT

←Older revision		Revision as of 20:59, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3h8e]] is a 2 chain structure ~~of [[Aminopeptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].	+	[[3h8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].

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

OCA: Protected "3h8e" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 12:14:51 GMT

Protected "3h8e" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:14, 27 July 2012

OCA at 12:14, 27 July 2012

OCA — Fri, 27 Jul 2012 12:14:49 GMT

←Older revision		Revision as of 12:14, 27 July 2012
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-	{{Seed}}
	[[Image:3h8e.png\|left\|200px]]		[[Image:3h8e.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3h8e", 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),
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	{{STRUCTURE_3h8e\| PDB=3h8e \| SCENE= }}		{{STRUCTURE_3h8e\| PDB=3h8e \| SCENE= }}

	===Low pH native structure of leucine aminopeptidase from Pseudomonas putida===		===Low pH native structure of leucine aminopeptidase from Pseudomonas putida===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20359484}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20359484 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_20359484}}		{{ABSTRACT_PUBMED_20359484}}

	==About this Structure==		==About this Structure==
-	~~3H8E~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].	+	[[3h8e]] is a 2 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].
		+
		+	==See Also==
		+	*[[Aminopeptidase\|Aminopeptidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20359484~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020359484</ref><references group="xtra"/>
	[[Category: Leucyl aminopeptidase]]		[[Category: Leucyl aminopeptidase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
Line 31:		Line 22:
	[[Category: Thunnissen, A M.W H]]		[[Category: Thunnissen, A M.W H]]
	[[Category: Aminopeptidase]]		[[Category: Aminopeptidase]]
-	[[Category: Cytoplasm]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Manganese]]		[[Category: Manganese]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Protease]]		[[Category: Protease]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:23:18 2010''

OCA at 04:18, 2 June 2010

OCA — Wed, 02 Jun 2010 04:18:51 GMT

←Older revision		Revision as of 04:18, 2 June 2010
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	{{Seed}}		{{Seed}}
-	[[Image:3h8e.~~jpg~~\|left\|200px]]	+	[[Image:3h8e.png\|left\|200px]]

	<!--		<!--
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	===Low pH native structure of leucine aminopeptidase from Pseudomonas putida===		===Low pH native structure of leucine aminopeptidase from Pseudomonas putida===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20359484}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20359484 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20359484}}

	==About this Structure==		==About this Structure==
	3H8E is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].		3H8E is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8E OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20359484</ref><references group="xtra"/>
	[[Category: Leucyl aminopeptidase]]		[[Category: Leucyl aminopeptidase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
Line 28:		Line 37:
	[[Category: Protease]]		[[Category: Protease]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Apr 14 09~~:49:27 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:23:18 2010''