1xrr - Revision history

OCA at 07:57, 15 May 2024

2024-05-15T07:57:25Z

←Older revision		Revision as of 07:57, 15 May 2024
Line 3:		Line 3:
	<StructureSection load='1xrr' size='340' side='right'caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1xrr' size='340' side='right'caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PRO:PROLINE'>PRO</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]] 2.4Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[1mtz\|1mtz]]~~, [[~~1mu0~~\|~~1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq~~]]~~</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>TA0830 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~2303~~ "~~Thermoplasma acidophila~~" ~~(sic) Darland et al. 1970])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [https://pdbe.org/1xrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [https://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [https://pdbe.org/1xrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [https://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.	+	[https://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 39:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Prolyl aminopeptidase~~]]	+	[[Category: Thermoplasma acidophilum]]
-	[[Category: Brandstetter, H]]	+	[[Category: Brandstetter H]]
-	[[Category: Goehring, W]]	+	[[Category: Goehring W]]
-	[[Category: Goettig, P]]	+	[[Category: Goettig P]]
-	[[Category: Groll, M]]	+	[[Category: Groll M]]
-	[[Category: Huber, R]]	+	[[Category: Huber R]]
-	[[Category: Kim, J S]]	+	[[Category: Kim J-S]]
-	[[Category: Konarev~~, P V~~]]	+	[[Category: Konarev PV]]
-	[[Category: Svergun~~, D I]]~~	+	[[Category: Svergun DI]]
-	~~[[Category: Alpha-beta hydrolase]]~~	+
-	~~[[Category: Caged active site]]~~	+
-	~~[[Category: Diproline]]~~	+
-	~~[[Category: Hydrogen bonded network]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Substrate recognition~~]]	+

OCA at 06:40, 10 November 2021

2021-11-10T06:40:08Z

OCA at 10:17, 6 January 2021

2021-01-06T10:17:34Z

←Older revision		Revision as of 10:17, 6 January 2021
Line 1:		Line 1:

	==Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro==		==Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro==
-	<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='1xrr' size='340' side='right'caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1XRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://pdbe.org/1xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://pdbe.org/1xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]	+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Prolyl aminopeptidase]]		[[Category: Prolyl aminopeptidase]]
	[[Category: Brandstetter, H]]		[[Category: Brandstetter, H]]

OCA at 07:31, 18 April 2018

2018-04-18T07:31:58Z

←Older revision		Revision as of 07:31, 18 April 2018
Line 1:		Line 1:
		+
	==Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro==		==Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro==
	<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://pdbe.org/1xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://pdbe.org/1xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xr/1xrr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xr/1xrr_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>
	</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=1xrr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 08:47, 11 September 2015

2015-09-11T08:47:29Z

←Older revision		Revision as of 08:47, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermoplasma_acidophilum Thermoplasma acidophilum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma ~~acidophilum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://pdbe.org/1xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1xrr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Prolyl aminopeptidase]]		[[Category: Prolyl aminopeptidase]]
-	[[Category: Thermoplasma acidophilum]]
	[[Category: Brandstetter, H]]		[[Category: Brandstetter, H]]
	[[Category: Goehring, W]]		[[Category: Goehring, W]]

OCA at 14:03, 25 December 2014

2014-12-25T14:03:39Z

←Older revision		Revision as of 14:03, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Prolyl aminopeptidase]]		[[Category: Prolyl aminopeptidase]]
	[[Category: Thermoplasma acidophilum]]		[[Category: Thermoplasma acidophilum]]
-	[[Category: Brandstetter, H.]]	+	[[Category: Brandstetter, H]]
-	[[Category: Goehring, W.]]	+	[[Category: Goehring, W]]
-	[[Category: Goettig, P.]]	+	[[Category: Goettig, P]]
-	[[Category: Groll, M.]]	+	[[Category: Groll, M]]
-	[[Category: Huber, R.]]	+	[[Category: Huber, R]]
-	[[Category: Kim, J S.]]	+	[[Category: Kim, J S]]
-	[[Category: Konarev, P V.]]	+	[[Category: Konarev, P V]]
-	[[Category: Svergun, D I.]]	+	[[Category: Svergun, D I]]
	[[Category: Alpha-beta hydrolase]]		[[Category: Alpha-beta hydrolase]]
	[[Category: Caged active site]]		[[Category: Caged active site]]

OCA at 23:02, 28 September 2014

2014-09-28T23:02:18Z

←Older revision		Revision as of 23:02, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1xrr.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro==
		+	<StructureSection load='1xrr' size='340' side='right' caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [http://www.ebi.ac.uk/pdbsum/1xrr 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/xr/1xrr_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 tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and catalysis displayed distinct activity patterns toward fluorogenic test substrates. Crystal structures of the mutant proteins complexed with peptides Phe-Leu, Pro-Pro, or Pro-Leu-Gly-Gly showed interaction of glutamates 213 and 245 with the N termini of the peptides and defined the S1 and S1' sites and the role of the catalytic residues. Evidence was found for processive peptide cleavage in the N-to-C direction, whereby the P1' product is translocated into the S1 site. A functional interaction of F1 with the tricorn protease was observed with the inactive F1 mutant G37A. Moreover, small angle x-ray scattering measurements for tricorn and inhibited F1 have been interpreted as formation of transient and substrate-induced complexes.

-	~~{{STRUCTURE_1xrr\| PDB=1xrr \| SCENE= }}~~	+	X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum.,Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:15994304<ref>PMID:15994304</ref>

-	~~===Crystal structure~~ of ~~active site F1-mutant E245Q soaked with peptide Pro-Pro===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15994304}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1xrr]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA].~~	+

	==See Also==		==See Also==
	*[[Aminopeptidase\|Aminopeptidase]]		*[[Aminopeptidase\|Aminopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015994304<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Prolyl aminopeptidase]]		[[Category: Prolyl aminopeptidase]]
	[[Category: Thermoplasma acidophilum]]		[[Category: Thermoplasma acidophilum]]

OCA at 17:35, 20 October 2012

2012-10-20T17:35:37Z

←Older revision		Revision as of 17:35, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1xrr]] is a 1 chain structure ~~of [[Aminopeptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA].	+	[[1xrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA].

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

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

2012-07-27T01:25:34Z

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

←Older revision

Revision as of 01:25, 27 July 2012

OCA at 01:25, 27 July 2012

2012-07-27T01:25:33Z

←Older revision		Revision as of 01:25, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1xrr.png\|left\|200px]]		[[Image:1xrr.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1xrr", 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_1xrr\| PDB=1xrr \| SCENE= }}		{{STRUCTURE_1xrr\| PDB=1xrr \| SCENE= }}

	===Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro===		===Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15994304}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15994304 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15994304}}		{{ABSTRACT_PUBMED_15994304}}

	==About this Structure==		==About this Structure==
-	~~1XRR~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA].	+	[[1xrr]] is a 1 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA].
		+
		+	==See Also==
		+	*[[Aminopeptidase\|Aminopeptidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15994304~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015994304</ref><references group="xtra"/>
	[[Category: Prolyl aminopeptidase]]		[[Category: Prolyl aminopeptidase]]
	[[Category: Thermoplasma acidophilum]]		[[Category: Thermoplasma acidophilum]]
Line 38:		Line 29:
	[[Category: Diproline]]		[[Category: Diproline]]
	[[Category: Hydrogen bonded network]]		[[Category: Hydrogen bonded network]]
		+	[[Category: Hydrolase]]
	[[Category: Substrate recognition]]		[[Category: Substrate recognition]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:11:02 2009''

←Older revision		Revision as of 06:40, 10 November 2021
Line 3:		Line 3:
	<StructureSection load='1xrr' size='340' side='right'caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1xrr' size='340' side='right'caption='[[1xrr]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1XRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mtz\|1mtz]], [[1mu0\|1mu0]], [[1mt3\|1mt3]], [[1xqv\|1xqv]], [[1xqw\|1xqw]], [[1xqx\|1xqx]], [[1xqy\|1xqy]], [[1xrl\|1xrl]], [[1xrm\|1xrm]], [[1xrn\|1xrn]], [[1xro\|1xro]], [[1xrp\|1xrp]], [[1xrq\|1xrq]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TA0830 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [~~http~~://pdbe.org/1xrr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr 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=1xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrr OCA], [https://pdbe.org/1xrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrr RCSB], [https://www.ebi.ac.uk/pdbsum/1xrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.	+	[[https://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]