2e02 - Revision history

OCA at 18:46, 29 May 2024

2024-05-29T18:46:35Z

← Older revision		Revision as of 18:46, 29 May 2024
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	<StructureSection load='2e02' size='340' side='right'caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2e02' size='340' side='right'caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E02 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E02 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;'>[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]]~~, [[~~2e03~~\|~~2e03]~~]~~</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]] 2.2Å</td></tr>
	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase~~]~~, with EC number [https://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [https://pdbe.org/2e02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [https://www.ebi.ac.uk/pdbsum/2e02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e02 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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [https://pdbe.org/2e02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [https://www.ebi.ac.uk/pdbsum/2e02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST]] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>		[https://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Proteinase\|Proteinase]]
	*[[Proteinase 3D structures\|Proteinase 3D structures]]		*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Atcc 18824]]~~
	~~[[Category: Bleomycin hydrolase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Farrell, P A.O~~]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Joshua-Tor, L]]		[[Category: Joshua-Tor L]]
	[[Category: ~~C1 protease]]~~		[[Category: O'Farrell PA]]
	~~[[Category: Hydrolase]]~~
	~~[[Category: Thiol protease~~]]

OCA at 06:52, 10 November 2021

2021-11-10T06:52:44Z

← Older revision		Revision as of 06:52, 10 November 2021
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	<StructureSection load='2e02' size='340' side='right'caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2e02' size='340' side='right'caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2E02 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E02 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</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;'>[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [~~http~~://pdbe.org/2e02 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2e02 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2e02 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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [https://pdbe.org/2e02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [https://www.ebi.ac.uk/pdbsum/2e02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST]] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>		[[https://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST]] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:24, 11 March 2020

2020-03-11T08:24:43Z

← Older revision		Revision as of 08:24, 11 March 2020
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	==Crystal structure of H369L mutant of yeast bleomycin hydrolase==		==Crystal structure of H369L mutant of yeast bleomycin hydrolase==
	<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2e02' size='340' side='right'caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 2e02" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2e02" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Proteinase\|Proteinase]]
			*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
			[[Category: Large Structures]]
	[[Category: Farrell, P A.O]]		[[Category: Farrell, P A.O]]
	[[Category: Joshua-Tor, L]]		[[Category: Joshua-Tor, L]]

OCA at 07:03, 6 June 2018

2018-06-06T07:03:49Z

← Older revision		Revision as of 07:03, 6 June 2018
Line 1:		Line 1:

	==Crystal structure of H369L mutant of yeast bleomycin hydrolase==		==Crystal structure of H369L mutant of yeast bleomycin hydrolase==
	<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://pdbe.org/2e02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://pdbe.org/2e02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/2e02_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/2e02_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 11:32, 7 February 2016

2016-02-07T11:32:47Z

← Older revision		Revision as of 11:32, 7 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e02 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:05, 10 September 2015

2015-09-10T01:05:22Z

← Older revision		Revision as of 01:05, 10 September 2015
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	<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://pdbe.org/2e02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2e02" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Atcc 18824]]
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
	~~[[Category: Saccharomyces cerevisiae]]~~
	[[Category: Farrell, P A.O]]		[[Category: Farrell, P A.O]]
	[[Category: Joshua-Tor, L]]		[[Category: Joshua-Tor, L]]

OCA at 14:45, 24 December 2014

2014-12-24T14:45:58Z

← Older revision		Revision as of 14:45, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/BLH1_YEAST BLH1_YEAST]] The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.<ref>PMID:12555812</ref> <ref>PMID:16769724</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Farrell, P A.O.]]		[[Category: Farrell, P A.O]]
	[[Category: Joshua-Tor, L~~.]]~~		[[Category: Joshua-Tor, L]]
	~~[[Category: Bleomycin hydrolase~~]]
	[[Category: C1 protease]]		[[Category: C1 protease]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Thiol protease]]		[[Category: Thiol protease]]

OCA at 00:23, 30 September 2014

2014-09-30T00:23:23Z

← Older revision		Revision as of 00:23, 30 September 2014
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	[[Image:~~2e02~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of H369L mutant of yeast bleomycin hydrolase==
			<StructureSection load='2e02' size='340' side='right' caption='[[2e02]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E02 FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dzy\|2dzy]], [[2dzz\|2dzz]], [[2e00\|2e00]], [[2e01\|2e01]], [[2e03\|2e03]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </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=2e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e02 RCSB], [http://www.ebi.ac.uk/pdbsum/2e02 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/e0/2e02_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 ==
			Bleomycin hydrolase (BH) is a hexameric papain family cysteine protease which is involved in preparing peptides for antigen presentation and has been implicated in tumour cell resistance to bleomycin chemotherapy. Structures of active-site mutants of yeast BH yielded unexpected results. Replacement of the active-site asparagine with alanine, valine or leucine results in the destabilization of the histidine side chain, demonstrating unambiguously the role of the asparagine residue in correctly positioning the histidine for catalysis. Replacement of the histidine with alanine or leucine destabilizes the asparagine position, indicating a delicate arrangement of the active-site residues. In all of the mutants, the C-terminus of the protein, which lies in the active site, protrudes further into the active site. All mutants were compromised in their catalytic activity. The structures also revealed the importance of a tightly bound water molecule which stabilizes a loop near the active site and which is conserved throughout the papain family. It is displaced in a number of the mutants, causing destabilization of this loop and a nearby loop, resulting in a large movement of the active-site cysteine. The results imply that this water molecule plays a key structural role in this family of enzymes.

	~~{{STRUCTURE_2e02\| PDB=2e02 \| SCENE= }}~~		Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure.,O'Farrell PA, Joshua-Tor L Biochem J. 2007 Jan 15;401(2):421-8. PMID:17007609<ref>PMID:17007609</ref>

	~~===Crystal structure of H369L mutant~~ of ~~yeast bleomycin hydrolase===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_17007609}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2e02]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:017007609<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA: Protected "2e02" [edit=sysop:move=sysop]

2013-01-06T09:46:42Z

Protected "2e02" [edit=sysop:move=sysop]

← Older revision	Revision as of 09:46, 6 January 2013
(No difference)

OCA at 09:46, 6 January 2013

2013-01-06T09:46:38Z

← Older revision		Revision as of 09:46, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2e02.png\|left\|200px]]		[[Image:2e02.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2e02", 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_2e02\| PDB=2e02 \| SCENE= }}		{{STRUCTURE_2e02\| PDB=2e02 \| SCENE= }}

	===Crystal structure of H369L mutant of yeast bleomycin hydrolase===		===Crystal structure of H369L mutant of yeast bleomycin hydrolase===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_17007609}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 17007609 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_17007609}}		{{ABSTRACT_PUBMED_17007609}}

	==About this Structure==		==About this Structure==
	~~2E02~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA].		[[2e02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E02 OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~17007609~~</ref><references group="xtra"/>		<ref group="xtra">PMID:017007609</ref><references group="xtra"/>
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
Line 30:		Line 18:
	[[Category: Bleomycin hydrolase]]		[[Category: Bleomycin hydrolase]]
	[[Category: C1 protease]]		[[Category: C1 protease]]
			[[Category: Hydrolase]]
	[[Category: Thiol protease]]		[[Category: Thiol protease]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:31:09 2009''~~