2ade - Revision history

OCA at 07:22, 23 August 2023

OCA — Wed, 23 Aug 2023 07:22:41 GMT

←Older revision		Revision as of 07:22, 23 August 2023
Line 1:		Line 1:

	==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==		==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==
-	<StructureSection load='2ade' size='340' side='right'caption='[[2ade]]' scene=''>	+	<StructureSection load='2ade' size='340' side='right'caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADE FirstGlance]. <br>
-	</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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [https://pdbe.org/2ade PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [https://www.ebi.ac.uk/pdbsum/2ade PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ade ProSAT]</span></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]] 2.65Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [https://pdbe.org/2ade PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [https://www.ebi.ac.uk/pdbsum/2ade PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ade ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q93X60_CICIN Q93X60_CICIN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 16:		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=2ade 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=2ade ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	* Invertases and fructan exohydrolases (FEHs) fulfil important physiological functions in plants. Sucrose is the typical substrate for invertases and bacterial levansucrases but not for plant FEHs, which are usually inhibited by sucrose. * Here we report on complexes between chicory (Cichorium intybus) 1-FEH IIa with the substrate 1-kestose and the inhibitors sucrose, fructose and 2,5 dideoxy-2,5-imino-D-mannitol. Comparisons with other family GH32 and 68 enzyme-substrate complexes revealed that sucrose can bind as a substrate (invertase/levansucrase) or as an inhibitor (1-FEH IIa). * Sucrose acts as inhibitor because the O2 of the glucose moiety forms an H-linkage with the acid-base catalyst E201, inhibiting catalysis. By contrast, the homologous O3 of the internal fructose in the substrate 1-kestose forms an intramolecular H-linkage and does not interfere with the catalytic process. Mutagenesis showed that W82 and S101 are important for binding sucrose as inhibitor. * The physiological implications of the essential differences in the active sites of FEHs and invertases/levansucrases are discussed. Sucrose-inhibited FEHs show a K(i) (inhibition constant) well below physiological sucrose concentrations and could be rapidly activated under carbon deprivation.
		+
		+	Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor.,Verhaest M, Lammens W, Le Roy K, De Ranter CJ, Van Laere A, Rabijns A, Van den Ende W New Phytol. 2007;174(1):90-100. PMID:17335500<ref>PMID:17335500</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2ade" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cichorium intybus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: De Ranter CJ]]		[[Category: De Ranter CJ]]

OCA at 11:31, 3 February 2021

OCA — Wed, 03 Feb 2021 11:31:19 GMT

←Older revision		Revision as of 11:31, 3 February 2021
Line 1:		Line 1:

	==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==		==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==
-	<StructureSection load='2ade' size='340' side='right' caption='[[2ade]]~~, [[Resolution\|resolution]] 2.65Å~~' scene=''>	+	<StructureSection load='2ade' size='340' side='right'caption='[[2ade]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cicin Cicin].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ADE FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [https://pdbe.org/2ade PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [https://www.ebi.ac.uk/pdbsum/2ade PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ade ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>~~	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 CICIN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [~~http~~://pdbe.org/2ade PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ade PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ade ProSAT]</span></td></tr>	+
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 20:		Line 16:
	</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=2ade 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=2ade ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	* Invertases and fructan exohydrolases (FEHs) fulfil important physiological functions in plants. Sucrose is the typical substrate for invertases and bacterial levansucrases but not for plant FEHs, which are usually inhibited by sucrose. * Here we report on complexes between chicory (Cichorium intybus) 1-FEH IIa with the substrate 1-kestose and the inhibitors sucrose, fructose and 2,5 dideoxy-2,5-imino-D-mannitol. Comparisons with other family GH32 and 68 enzyme-substrate complexes revealed that sucrose can bind as a substrate (invertase/levansucrase) or as an inhibitor (1-FEH IIa). * Sucrose acts as inhibitor because the O2 of the glucose moiety forms an H-linkage with the acid-base catalyst E201, inhibiting catalysis. By contrast, the homologous O3 of the internal fructose in the substrate 1-kestose forms an intramolecular H-linkage and does not interfere with the catalytic process. Mutagenesis showed that W82 and S101 are important for binding sucrose as inhibitor. * The physiological implications of the essential differences in the active sites of FEHs and invertases/levansucrases are discussed. Sucrose-inhibited FEHs show a K(i) (inhibition constant) well below physiological sucrose concentrations and could be rapidly activated under carbon deprivation.
-
-	Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor.,Verhaest M, Lammens W, Le Roy K, De Ranter CJ, Van Laere A, Rabijns A, Van den Ende W New Phytol. 2007;174(1):90-100. PMID:17335500<ref>PMID:17335500</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2ade" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cicin~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Ende, W Van den~~]]	+	[[Category: De Ranter CJ]]
-	[[Category: ~~Laere, A Van~~]]	+	[[Category: Le Roy K]]
-	[[Category: Rabijns, A]]	+	[[Category: Rabijns A]]
-	[[Category: ~~Ranter, C J.De~~]]	+	[[Category: Van Laere A]]
-	[[Category: ~~Roy, K Le~~]]	+	[[Category: Van den Ende W]]
-	[[Category: Verhaest, M]]	+	[[Category: Verhaest M]]
-	~~[[Category: Five fold beta propeller]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:06, 9 May 2018

OCA — Wed, 09 May 2018 07:06:56 GMT

←Older revision		Revision as of 07:06, 9 May 2018
Line 1:		Line 1:
		+
	==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==		==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==
	<StructureSection load='2ade' size='340' side='right' caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='2ade' size='340' side='right' caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 CICIN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 CICIN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://pdbe.org/2ade PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade 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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://pdbe.org/2ade PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ade ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2ade_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2ade_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=2ade ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:21, 11 September 2015

OCA — Fri, 11 Sep 2015 15:21:27 GMT

←Older revision		Revision as of 15:21, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2ade' size='340' side='right' caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='2ade' size='340' side='right' caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Cichorium_intybus Cichorium intybus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cicin Cicin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 ~~Cichorium intybus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 CICIN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade 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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://pdbe.org/2ade PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 27:		Line 27:
	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 2ade" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cichorium intybus~~]]	+	[[Category: Cicin]]
	[[Category: Ende, W Van den]]		[[Category: Ende, W Van den]]
	[[Category: Laere, A Van]]		[[Category: Laere, A Van]]

OCA at 09:25, 8 January 2015

OCA — Thu, 08 Jan 2015 09:25:37 GMT

←Older revision		Revision as of 09:25, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 Cichorium intybus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 Cichorium intybus])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade 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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade 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 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Cichorium intybus]]		[[Category: Cichorium intybus]]
-	[[Category: Ende, W Van den.]]	+	[[Category: Ende, W Van den]]
-	[[Category: Laere, A Van.]]	+	[[Category: Laere, A Van]]
-	[[Category: Rabijns, A.]]	+	[[Category: Rabijns, A]]
-	[[Category: Ranter, C J.De.]]	+	[[Category: Ranter, C J.De]]
-	[[Category: Roy, K Le.]]	+	[[Category: Roy, K Le]]
-	[[Category: Verhaest, M.]]	+	[[Category: Verhaest, M]]
	[[Category: Five fold beta propeller]]		[[Category: Five fold beta propeller]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 01:55, 30 September 2014

OCA — Tue, 30 Sep 2014 01:55:17 GMT

←Older revision		Revision as of 01:55, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2ade.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose==
		+	<StructureSection load='2ade' size='340' side='right' caption='[[2ade]], [[Resolution\|resolution]] 2.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADE FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2add\|2add]], [[2aez\|2aez]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1-FEH IIa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13427 Cichorium intybus])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructan_beta-(2,1)-fructosidase Fructan beta-(2,1)-fructosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.153 3.2.1.153] </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=2ade FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ade OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ade RCSB], [http://www.ebi.ac.uk/pdbsum/2ade 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/ad/2ade_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 ==
		+	* Invertases and fructan exohydrolases (FEHs) fulfil important physiological functions in plants. Sucrose is the typical substrate for invertases and bacterial levansucrases but not for plant FEHs, which are usually inhibited by sucrose. * Here we report on complexes between chicory (Cichorium intybus) 1-FEH IIa with the substrate 1-kestose and the inhibitors sucrose, fructose and 2,5 dideoxy-2,5-imino-D-mannitol. Comparisons with other family GH32 and 68 enzyme-substrate complexes revealed that sucrose can bind as a substrate (invertase/levansucrase) or as an inhibitor (1-FEH IIa). * Sucrose acts as inhibitor because the O2 of the glucose moiety forms an H-linkage with the acid-base catalyst E201, inhibiting catalysis. By contrast, the homologous O3 of the internal fructose in the substrate 1-kestose forms an intramolecular H-linkage and does not interfere with the catalytic process. Mutagenesis showed that W82 and S101 are important for binding sucrose as inhibitor. * The physiological implications of the essential differences in the active sites of FEHs and invertases/levansucrases are discussed. Sucrose-inhibited FEHs show a K(i) (inhibition constant) well below physiological sucrose concentrations and could be rapidly activated under carbon deprivation.

-	~~{{STRUCTURE_2ade\| PDB=2ade \| SCENE= }}~~	+	Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor.,Verhaest M, Lammens W, Le Roy K, De Ranter CJ, Van Laere A, Rabijns A, Van den Ende W New Phytol. 2007;174(1):90-100. PMID:17335500<ref>PMID:17335500</ref>

-	~~===Crystal structure~~ of ~~fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17335500}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2ade]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Cichorium_intybus Cichorium intybus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:017335500<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Cichorium intybus]]		[[Category: Cichorium intybus]]
	[[Category: Ende, W Van den.]]		[[Category: Ende, W Van den.]]

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

OCA — Sun, 06 Jan 2013 11:08:37 GMT

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

←Older revision

Revision as of 11:08, 6 January 2013

OCA at 11:08, 6 January 2013

OCA — Sun, 06 Jan 2013 11:08:35 GMT

←Older revision		Revision as of 11:08, 6 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2ade.png\|left\|200px]]		[[Image:2ade.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2ade", 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_2ade\| PDB=2ade \| SCENE= }}		{{STRUCTURE_2ade\| PDB=2ade \| SCENE= }}

	===Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose===		===Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17335500}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17335500 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17335500}}		{{ABSTRACT_PUBMED_17335500}}

	==About this Structure==		==About this Structure==
-	~~2ADE~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].	+	[[2ade]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17335500~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017335500</ref><references group="xtra"/>
	[[Category: Cichorium intybus]]		[[Category: Cichorium intybus]]
	[[Category: Ende, W Van den.]]		[[Category: Ende, W Van den.]]
Line 33:		Line 21:
	[[Category: Five fold beta propeller]]		[[Category: Five fold beta propeller]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:57:58 2009''

OCA at 23:58, 17 February 2009

OCA — Tue, 17 Feb 2009 23:58:01 GMT

←Older revision		Revision as of 23:58, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2ADE is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].	+	2ADE is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].

	==Reference==		==Reference==
-	Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor., Verhaest M, Lammens W, Le Roy K, De Ranter CJ, Van Laere A, Rabijns A, Van den Ende W, New Phytol. 2007;174(1):90-100. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/17335500 17335500]~~	+	<ref group="xtra">PMID:17335500</ref><references group="xtra"/>
	[[Category: Cichorium intybus]]		[[Category: Cichorium intybus]]
-	[[Category: Single protein]]
	[[Category: Ende, W Van den.]]		[[Category: Ende, W Van den.]]
	[[Category: Laere, A Van.]]		[[Category: Laere, A Van.]]
Line 35:		Line 34:
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Sep 24 09~~:02:~~42 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:57:58 2009''

OCA at 06:02, 24 September 2008

OCA — Wed, 24 Sep 2008 06:02:42 GMT

←Older revision		Revision as of 06:02, 24 September 2008
Line 1:		Line 1:
-	[[Image:2ade.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2ade.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2ade\| PDB=2ade \| SCENE= }}		{{STRUCTURE_2ade\| PDB=2ade \| SCENE= }}

-	~~'''~~Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose~~'''~~	+	===Crystal structure of fructan 1-exohydrolase IIa from Cichorium intybus in complex with fructose===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_17335500}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 17335500 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_17335500}}

	==About this Structure==		==About this Structure==
	2ADE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].		2ADE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cichorium_intybus Cichorium intybus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADE OCA].
		+
		+	==Reference==
		+	Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor., Verhaest M, Lammens W, Le Roy K, De Ranter CJ, Van Laere A, Rabijns A, Van den Ende W, New Phytol. 2007;174(1):90-100. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17335500 17335500]
	[[Category: Cichorium intybus]]		[[Category: Cichorium intybus]]
	[[Category: Single protein]]		[[Category: Single protein]]
Line 19:		Line 29:
	[[Category: Laere, A Van.]]		[[Category: Laere, A Van.]]
	[[Category: Rabijns, A.]]		[[Category: Rabijns, A.]]
-	[[Category: Ranter, C De.]]	+	[[Category: Ranter, C J.De.]]
	[[Category: Roy, K Le.]]		[[Category: Roy, K Le.]]
	[[Category: Verhaest, M.]]		[[Category: Verhaest, M.]]
	[[Category: Five fold beta propeller]]		[[Category: Five fold beta propeller]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 18~~:54:21 2008''	+	[[Category: Hydrolase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 24 09:02:42 2008''