2o7v - Revision history

OCA at 05:23, 17 October 2024

2024-10-17T05:23:37Z

← Older revision		Revision as of 05:23, 17 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7v_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7v_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2o7v 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=2o7v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Carboxylesterases (CXEs) are widely distributed in plants, where they have been implicated in roles that include plant defense, plant development, and secondary metabolism. We have cloned, overexpressed, purified, and crystallized a carboxylesterase from the kiwifruit species Actinidia eriantha (AeCXE1). The structure of AeCXE1 was determined by X-ray crystallography at 1.4 A resolution. The crystal structure revealed that AeCXE1 is a member of the alpha/beta-hydrolase fold superfamily, most closely related structurally to the hormone-sensitive lipase subgroup. The active site of the enzyme, located in an 11 A deep hydrophobic gorge, contains the conserved catalytic triad residues Ser169, Asp276, and His306. Kinetic analysis using artificial ester substrates showed that the enzyme can hydrolyze a range of carboxylester substrates with acyl groups ranging from C2 to C16, with a preference for butyryl moieties. This preference was supported by the discovery of a three-carbon acyl adduct bound to the active site Ser169 in the native structure. AeCXE1 was also found to be inhibited by organophosphates, with paraoxon (IC50 = 1.1 muM) a more potent inhibitor than dimethylchlorophosphate (DMCP; IC50 = 9.2 muM). The structure of AeCXE1 with paraoxon bound was determined at 2.3 A resolution and revealed that the inhibitor binds covalently to the catalytic serine residue, with virtually no change in the structure of the enzyme. The structural information for AeCXE1 provides a basis for addressing the wider functional roles of carboxylesterases in plants.

			High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon.,Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN Biochemistry. 2007 Feb 20;46(7):1851-9. Epub 2007 Jan 26. PMID:17256879<ref>PMID:17256879</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 2o7v" style="background-color:#fffaf0;"></div>

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

OCA at 06:28, 3 April 2024

2024-04-03T06:28:57Z

← Older revision		Revision as of 06:28, 3 April 2024
Line 20:		Line 20:
	</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=2o7v 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=2o7v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Carboxylesterases (CXEs) are widely distributed in plants, where they have been implicated in roles that include plant defense, plant development, and secondary metabolism. We have cloned, overexpressed, purified, and crystallized a carboxylesterase from the kiwifruit species Actinidia eriantha (AeCXE1). The structure of AeCXE1 was determined by X-ray crystallography at 1.4 A resolution. The crystal structure revealed that AeCXE1 is a member of the alpha/beta-hydrolase fold superfamily, most closely related structurally to the hormone-sensitive lipase subgroup. The active site of the enzyme, located in an 11 A deep hydrophobic gorge, contains the conserved catalytic triad residues Ser169, Asp276, and His306. Kinetic analysis using artificial ester substrates showed that the enzyme can hydrolyze a range of carboxylester substrates with acyl groups ranging from C2 to C16, with a preference for butyryl moieties. This preference was supported by the discovery of a three-carbon acyl adduct bound to the active site Ser169 in the native structure. AeCXE1 was also found to be inhibited by organophosphates, with paraoxon (IC50 = 1.1 muM) a more potent inhibitor than dimethylchlorophosphate (DMCP; IC50 = 9.2 muM). The structure of AeCXE1 with paraoxon bound was determined at 2.3 A resolution and revealed that the inhibitor binds covalently to the catalytic serine residue, with virtually no change in the structure of the enzyme. The structural information for AeCXE1 provides a basis for addressing the wider functional roles of carboxylesterases in plants.

	High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon.,Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN Biochemistry. 2007 Feb 20;46(7):1851-9. Epub 2007 Jan 26. PMID:17256879<ref>PMID:17256879</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2o7v" style="background-color:#fffaf0;"></div>~~

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

OCA at 00:15, 28 December 2023

2023-12-28T00:15:25Z

← Older revision		Revision as of 00:15, 28 December 2023
Line 3:		Line 3:
	<StructureSection load='2o7v' size='340' side='right'caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2o7v' size='340' side='right'caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Acter Acter~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</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]] 2.3Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em~~;~~'>[[2o7r\|2o7r]]</div>~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CXE1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~165200 ACTER])</td~~><~~/tr>~~
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1]~~ </~~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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [https://pdbe.org/2o7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [https://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v 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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [https://pdbe.org/2o7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [https://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER]] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>		[https://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Acter]]~~		[[Category: Actinidia eriantha]]
	~~[[Category: Carboxylesterase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Baker~~, E N~~]]		[[Category: Baker EN]]
	[[Category: Baker~~, H M~~]]		[[Category: Baker HM]]
	[[Category: Ileperuma~~, N R~~]]		[[Category: Ileperuma NR]]
	[[Category: Marshall~~, S D~~]]		[[Category: Marshall SD]]
	[[Category: Newcomb~~, R D~~]]		[[Category: Newcomb RD]]
	[[Category: Oakeshott~~, J G~~]]		[[Category: Oakeshott JG]]
	[[Category: Plummer~~, K M~~]]		[[Category: Plummer KM]]
	[[Category: Russell~~, R J~~]]		[[Category: Russell RJ]]
	[[Category: Squire~~, C J]]~~		[[Category: Squire CJ]]
	~~[[Category: Actinidia eriantha]]~~
	~~[[Category: Aecxe1]]~~
	~~[[Category: Alpha/beta hydrolase]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Insecticide]]~~
	~~[[Category: Paraoxon~~]]

OCA at 16:02, 8 June 2021

2021-06-08T16:02:29Z

← Older revision		Revision as of 16:02, 8 June 2021
Line 1:		Line 1:

	==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==		==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==
	<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2o7v' size='340' side='right'caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Acter Acter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2O7V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acter Acter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2o7r\|2o7r]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [~~http~~://pdbe.org/2o7v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v 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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [https://pdbe.org/2o7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [https://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER]] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>		[[https://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER]] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7v_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7v_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 33:		Line 33:

	==See Also==		==See Also==
	*[[Carboxylesterase\|Carboxylesterase]]		*[[Carboxylesterase 3D structures\|Carboxylesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Acter]]		[[Category: Acter]]
	[[Category: Carboxylesterase]]		[[Category: Carboxylesterase]]
			[[Category: Large Structures]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Baker, H M]]		[[Category: Baker, H M]]

OCA at 08:53, 18 October 2017

2017-10-18T08:53:37Z

← Older revision		Revision as of 08:53, 18 October 2017
Line 1:		Line 1:

	==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==		==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==
	<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://pdbe.org/2o7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v 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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://pdbe.org/2o7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=2o7v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:24, 11 September 2015

2015-09-11T11:24:24Z

← Older revision		Revision as of 11:24, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Actinidia_eriantha Actinidia eriantha~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acter Acter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ~~Actinidia eriantha~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 ACTER])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v 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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://pdbe.org/2o7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/CXE1_ACTER CXE1_ACTER]] Carboxylesterase acting on esters with varying acyl chain length.<ref>PMID:17256879</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		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 2o7v" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Actinidia eriantha~~]]		[[Category: Acter]]
	[[Category: Carboxylesterase]]		[[Category: Carboxylesterase]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
Line 45:		Line 48:
	[[Category: Russell, R J]]		[[Category: Russell, R J]]
	[[Category: Squire, C J]]		[[Category: Squire, C J]]
			[[Category: Actinidia eriantha]]
	[[Category: Aecxe1]]		[[Category: Aecxe1]]
	[[Category: Alpha/beta hydrolase]]		[[Category: Alpha/beta hydrolase]]

OCA at 15:25, 19 January 2015

2015-01-19T15:25:18Z

← Older revision		Revision as of 15:25, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 Actinidia eriantha])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 Actinidia eriantha])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v 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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	[[Category: Actinidia eriantha]]		[[Category: Actinidia eriantha]]
	[[Category: Carboxylesterase]]		[[Category: Carboxylesterase]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N]]
	[[Category: Baker, H M.]]		[[Category: Baker, H M]]
	[[Category: Ileperuma, N R.]]		[[Category: Ileperuma, N R]]
	[[Category: Marshall, S D.]]		[[Category: Marshall, S D]]
	[[Category: Newcomb, R D.]]		[[Category: Newcomb, R D]]
	[[Category: Oakeshott, J G.]]		[[Category: Oakeshott, J G]]
	[[Category: Plummer, K M.]]		[[Category: Plummer, K M]]
	[[Category: Russell, R J.]]		[[Category: Russell, R J]]
	[[Category: Squire, C J~~.]]~~		[[Category: Squire, C J]]
	~~[[Category: Actinidia eriantha~~]]
	[[Category: Aecxe1]]		[[Category: Aecxe1]]
	[[Category: Alpha/beta hydrolase]]		[[Category: Alpha/beta hydrolase]]
	~~[[Category: Carboxylesterase]]~~
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Insecticide]]		[[Category: Insecticide]]
	[[Category: Paraoxon]]		[[Category: Paraoxon]]

OCA at 18:46, 30 September 2014

2014-09-30T18:46:50Z

← Older revision		Revision as of 18:46, 30 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2o7v~~\| ~~PDB~~=2o7v \| ~~SCENE~~= }}		==Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon==
	===Carboxylesterase ~~AeCXE1~~ from Actinidia eriantha ~~covalently~~ inhibited by paraoxon===		<StructureSection load='2o7v' size='340' side='right' caption='[[2o7v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	~~{{ABSTRACT_PUBMED_17256879}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7V FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEP:DIETHYL+PHOSPHONATE'>DEP</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o7r\|2o7r]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CXE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=165200 Actinidia eriantha])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=2o7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7v RCSB], [http://www.ebi.ac.uk/pdbsum/2o7v 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/o7/2o7v_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 ==
			Carboxylesterases (CXEs) are widely distributed in plants, where they have been implicated in roles that include plant defense, plant development, and secondary metabolism. We have cloned, overexpressed, purified, and crystallized a carboxylesterase from the kiwifruit species Actinidia eriantha (AeCXE1). The structure of AeCXE1 was determined by X-ray crystallography at 1.4 A resolution. The crystal structure revealed that AeCXE1 is a member of the alpha/beta-hydrolase fold superfamily, most closely related structurally to the hormone-sensitive lipase subgroup. The active site of the enzyme, located in an 11 A deep hydrophobic gorge, contains the conserved catalytic triad residues Ser169, Asp276, and His306. Kinetic analysis using artificial ester substrates showed that the enzyme can hydrolyze a range of carboxylester substrates with acyl groups ranging from C2 to C16, with a preference for butyryl moieties. This preference was supported by the discovery of a three-carbon acyl adduct bound to the active site Ser169 in the native structure. AeCXE1 was also found to be inhibited by organophosphates, with paraoxon (IC50 = 1.1 muM) a more potent inhibitor than dimethylchlorophosphate (DMCP; IC50 = 9.2 muM). The structure of AeCXE1 with paraoxon bound was determined at 2.3 A resolution and revealed that the inhibitor binds covalently to the catalytic serine residue, with virtually no change in the structure of the enzyme. The structural information for AeCXE1 provides a basis for addressing the wider functional roles of carboxylesterases in plants.

	~~==About this Structure==~~		High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon.,Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN Biochemistry. 2007 Feb 20;46(7):1851-9. Epub 2007 Jan 26. PMID:17256879<ref>PMID:17256879</ref>
	~~[[2o7v]] is a 1 chain~~ structure with ~~sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2O7V OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==See Also==		==See Also==
	*[[Carboxylesterase\|Carboxylesterase]]		*[[Carboxylesterase\|Carboxylesterase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:017256879<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Actinidia eriantha]]		[[Category: Actinidia eriantha]]
	[[Category: Carboxylesterase]]		[[Category: Carboxylesterase]]

OCA at 09:52, 11 March 2013

2013-03-11T09:52:30Z

← Older revision		Revision as of 09:52, 11 March 2013
Line 1:		Line 1:
	~~[[Image:2o7v.png\|left\|200px]]~~

	{{STRUCTURE_2o7v\| PDB=2o7v \| SCENE= }}		{{STRUCTURE_2o7v\| PDB=2o7v \| SCENE= }}

	===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===		===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===

	{{ABSTRACT_PUBMED_17256879}}		{{ABSTRACT_PUBMED_17256879}}

OCA at 13:18, 30 January 2013

2013-01-30T13:18:24Z

← Older revision		Revision as of 13:18, 30 January 2013
Line 1:		Line 1:
	[[Image:2o7v.png\|left\|200px]]		[[Image:2o7v.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2o7v", 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_2o7v\| PDB=2o7v \| SCENE= }}		{{STRUCTURE_2o7v\| PDB=2o7v \| SCENE= }}

	===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===		===Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_17256879}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 17256879 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_17256879}}		{{ABSTRACT_PUBMED_17256879}}

	==About this Structure==		==About this Structure==
	[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA].		[[2o7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinidia_eriantha Actinidia eriantha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7V OCA].

			==See Also==
			*[[Carboxylesterase\|Carboxylesterase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~17256879~~</ref><references group="xtra"/>		<ref group="xtra">PMID:017256879</ref><references group="xtra"/>
	[[Category: Actinidia eriantha]]		[[Category: Actinidia eriantha]]
	[[Category: Carboxylesterase]]		[[Category: Carboxylesterase]]
Line 34:		Line 26:
	[[Category: Russell, R J.]]		[[Category: Russell, R J.]]
	[[Category: Squire, C J.]]		[[Category: Squire, C J.]]
			[[Category: Actinidia eriantha]]
			[[Category: Aecxe1]]
			[[Category: Alpha/beta hydrolase]]
			[[Category: Carboxylesterase]]
			[[Category: Hydrolase]]
			[[Category: Insecticide]]
			[[Category: Paraoxon]]