2glx - Revision history

OCA at 13:51, 13 March 2024

OCA — Wed, 13 Mar 2024 13:51:58 GMT

←Older revision		Revision as of 13:51, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='2glx' size='340' side='right'caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2glx' size='340' side='right'caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_33212 Atcc 33212~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>~~, ~~<scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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]] 2.2Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>afr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~106592 ATCC 33212])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/1,5~~-~~anhydro~~-D-~~fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263]~~ </~~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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [https://pdbe.org/2glx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [https://www.ebi.ac.uk/pdbsum/2glx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx 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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [https://pdbe.org/2glx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [https://www.ebi.ac.uk/pdbsum/2glx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD]] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.	+	[https://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		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=2glx 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=2glx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Recombinant 1,5-anhydro-d-fructose reductase (AFR) from Sinorhizobium morelense S-30.7.5 was crystallized in complex with the cofactor NADP(H) and its structure determined to 2.2 A resolution using selenomethionine SAD (refined R(work) and R(free) factors of 18.9 and 25.0%, respectively). As predicted from the sequence and shown by the structure, AFR can be assigned to the GFO/IDH/MocA protein family. AFR consists of two domains. The N-terminal domain displays a Rossmann fold and contains the cofactor binding site. The intact crystals contain the oxidized cofactor NADP(+), whose attachment to the cofactor binding site is similar to that of NADP(+) in glucose-fructose oxidoreductase (GFOR) from Zymomonas mobilis. Due to variations in length and sequence within loop regions L3 and L5, respectively, the adenine moiety of NADP(+) adopts a different orientation in AFR caused by residue Arg38 forming hydrogen bonds with the 2'-phosphate moiety of NADP(+) and cation-pi stacking interactions with the adenine ring. Amino acid replacements in AFR (S10G, A13G, and S33D) showed that Ala13 is crucial for the discrimination between NADPH and NADH and yielded the A13G variant with dual cosubstrate specificity. The C-terminal domain contains the putative substrate binding site that was occupied by an acetate ion. As determined by analogy to GFOR and by site-directed mutagenesis of K94G, D176A, and H180A, residues Lys94, Asp176, and His180 are most likely involved in substrate binding and catalysis, as substitution of any of these residues resulted in a significant decrease in k(cat) for 1,5-AF. In this context, His180 might serve as a general acid-base catalyst by polarizing the carbonyl function of 1,5-AF to enable the transfer of the hydride from NADPH to the substrate. Here we present the first structure of an AFR enzyme catalyzing the stereoselective reduction of 1,5-AF to 1,5-anhydro-d-mannitol, the final step of a modified anhydrofructose pathway in S. morelense S-30.7.5. We also emphasize the importance of the A13G variant in biocatalysis for the synthesis of 1,5-AM and related derivatives.
-
-	Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis.,Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ Biochemistry. 2006 Aug 22;45(33):10030-42. PMID:16906761<ref>PMID:16906761</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2glx" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~1,5-anhydro-D-fructose reductase]]~~	+	[[Category: Ensifer adhaerens]]
-	~~[[Category: Atcc 33212~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dambe~~, T R~~]]	+	[[Category: Dambe TR]]
-	[[Category: Scheidig~~, A J]]~~	+	[[Category: Scheidig AJ]]
-	~~[[Category: 5-anhydro-d-fructose]]~~	+
-	~~[[Category: 5-anhydro-d-fructose reductase]]~~	+
-	~~[[Category: 5-anhydro-d-mannitol]]~~	+
-	~~[[Category: Bacterial 1]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Rossmann-fold]]~~	+
-	~~[[Category: Sugar metabolism~~]]	+

OCA at 19:09, 10 March 2021

OCA — Wed, 10 Mar 2021 19:09:01 GMT

←Older revision		Revision as of 19:09, 10 March 2021
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	==Crystal Structure Analysis of bacterial 1,5-AF Reductase==		==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
-	<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='2glx' size='340' side='right'caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_33212 Atcc 33212]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2GLX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33212 Atcc 33212]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [~~http~~://pdbe.org/2glx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2glx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx 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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [https://pdbe.org/2glx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [https://www.ebi.ac.uk/pdbsum/2glx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD]] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.	+	[[https://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD]] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.
	== 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/gl/2glx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/2glx_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 36:		Line 36:
	[[Category: 1,5-anhydro-D-fructose reductase]]		[[Category: 1,5-anhydro-D-fructose reductase]]
	[[Category: Atcc 33212]]		[[Category: Atcc 33212]]
		+	[[Category: Large Structures]]
	[[Category: Dambe, T R]]		[[Category: Dambe, T R]]
	[[Category: Scheidig, A J]]		[[Category: Scheidig, A J]]

OCA at 07:56, 18 October 2017

OCA — Wed, 18 Oct 2017 07:56:13 GMT

←Older revision		Revision as of 07:56, 18 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure Analysis of bacterial 1,5-AF Reductase==		==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
	<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://pdbe.org/2glx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx 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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://pdbe.org/2glx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2glx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 00:47, 8 February 2016

OCA — Mon, 08 Feb 2016 00:47:07 GMT

←Older revision		Revision as of 00:47, 8 February 2016
Line 18:		Line 18:
	<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=2glx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:19, 10 September 2015

OCA — Thu, 10 Sep 2015 06:19:34 GMT

←Older revision		Revision as of 06:19, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ensifer_adhaerens Ensifer adhaerens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33212 Atcc 33212]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ~~Ensifer adhaerens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 ATCC 33212])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx 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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://pdbe.org/2glx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 2glx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: 1,5-anhydro-D-fructose reductase]]		[[Category: 1,5-anhydro-D-fructose reductase]]
-	[[Category: ~~Ensifer adhaerens~~]]	+	[[Category: Atcc 33212]]
	[[Category: Dambe, T R]]		[[Category: Dambe, T R]]
	[[Category: Scheidig, A J]]		[[Category: Scheidig, A J]]

OCA at 19:20, 24 December 2014

OCA — Wed, 24 Dec 2014 19:20:02 GMT

←Older revision		Revision as of 19:20, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 Ensifer adhaerens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 Ensifer adhaerens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx 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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AFR_ENSAD AFR_ENSAD]] Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: 1,5-anhydro-D-fructose reductase]]		[[Category: 1,5-anhydro-D-fructose reductase]]
	[[Category: Ensifer adhaerens]]		[[Category: Ensifer adhaerens]]
-	[[Category: Dambe, T R.]]	+	[[Category: Dambe, T R]]
-	[[Category: Scheidig, A J.]]	+	[[Category: Scheidig, A J]]
	[[Category: 5-anhydro-d-fructose]]		[[Category: 5-anhydro-d-fructose]]
	[[Category: 5-anhydro-d-fructose reductase]]		[[Category: 5-anhydro-d-fructose reductase]]

OCA at 10:37, 30 September 2014

OCA — Tue, 30 Sep 2014 10:37:20 GMT

←Older revision		Revision as of 10:37, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2glx.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure Analysis of bacterial 1,5-AF Reductase==
		+	<StructureSection load='2glx' size='340' side='right' caption='[[2glx]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GLX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">afr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106592 Ensifer adhaerens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,5-anhydro-D-fructose_reductase 1,5-anhydro-D-fructose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.263 1.1.1.263] </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=2glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2glx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2glx RCSB], [http://www.ebi.ac.uk/pdbsum/2glx 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/gl/2glx_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 ==
		+	Recombinant 1,5-anhydro-d-fructose reductase (AFR) from Sinorhizobium morelense S-30.7.5 was crystallized in complex with the cofactor NADP(H) and its structure determined to 2.2 A resolution using selenomethionine SAD (refined R(work) and R(free) factors of 18.9 and 25.0%, respectively). As predicted from the sequence and shown by the structure, AFR can be assigned to the GFO/IDH/MocA protein family. AFR consists of two domains. The N-terminal domain displays a Rossmann fold and contains the cofactor binding site. The intact crystals contain the oxidized cofactor NADP(+), whose attachment to the cofactor binding site is similar to that of NADP(+) in glucose-fructose oxidoreductase (GFOR) from Zymomonas mobilis. Due to variations in length and sequence within loop regions L3 and L5, respectively, the adenine moiety of NADP(+) adopts a different orientation in AFR caused by residue Arg38 forming hydrogen bonds with the 2'-phosphate moiety of NADP(+) and cation-pi stacking interactions with the adenine ring. Amino acid replacements in AFR (S10G, A13G, and S33D) showed that Ala13 is crucial for the discrimination between NADPH and NADH and yielded the A13G variant with dual cosubstrate specificity. The C-terminal domain contains the putative substrate binding site that was occupied by an acetate ion. As determined by analogy to GFOR and by site-directed mutagenesis of K94G, D176A, and H180A, residues Lys94, Asp176, and His180 are most likely involved in substrate binding and catalysis, as substitution of any of these residues resulted in a significant decrease in k(cat) for 1,5-AF. In this context, His180 might serve as a general acid-base catalyst by polarizing the carbonyl function of 1,5-AF to enable the transfer of the hydride from NADPH to the substrate. Here we present the first structure of an AFR enzyme catalyzing the stereoselective reduction of 1,5-AF to 1,5-anhydro-d-mannitol, the final step of a modified anhydrofructose pathway in S. morelense S-30.7.5. We also emphasize the importance of the A13G variant in biocatalysis for the synthesis of 1,5-AM and related derivatives.

-	~~{{STRUCTURE_2glx\| PDB=2glx \| SCENE= }}~~	+	Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis.,Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ Biochemistry. 2006 Aug 22;45(33):10030-42. PMID:16906761<ref>PMID:16906761</ref>

-	~~===Crystal Structure Analysis of bacterial 1~~,~~5-AF Reductase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16906761}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2glx]] is~~ a ~~6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Ensifer_adhaerens Ensifer adhaerens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016906761<~~/~~ref~~><~~ref group="xtra">PMID:016461673</ref><references group="xtra"~~/>	+
	[[Category: 1,5-anhydro-D-fructose reductase]]		[[Category: 1,5-anhydro-D-fructose reductase]]
	[[Category: Ensifer adhaerens]]		[[Category: Ensifer adhaerens]]

OCA at 12:35, 23 January 2013

OCA — Wed, 23 Jan 2013 12:35:58 GMT

←Older revision		Revision as of 12:35, 23 January 2013
Line 1:		Line 1:
	[[Image:2glx.png\|left\|200px]]		[[Image:2glx.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2glx", 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_2glx\| PDB=2glx \| SCENE= }}		{{STRUCTURE_2glx\| PDB=2glx \| SCENE= }}

	===Crystal Structure Analysis of bacterial 1,5-AF Reductase===		===Crystal Structure Analysis of bacterial 1,5-AF Reductase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16906761}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16906761 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16906761}}		{{ABSTRACT_PUBMED_16906761}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16906761~~</ref><ref group="xtra">PMID:~~16461673~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016906761</ref><ref group="xtra">PMID:016461673</ref><references group="xtra"/>
	[[Category: 1,5-anhydro-D-fructose reductase]]		[[Category: 1,5-anhydro-D-fructose reductase]]
	[[Category: Ensifer adhaerens]]		[[Category: Ensifer adhaerens]]

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

OCA — Mon, 14 Mar 2011 23:43:48 GMT

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

←Older revision

Revision as of 23:43, 14 March 2011

OCA at 23:43, 14 March 2011

OCA — Mon, 14 Mar 2011 23:43:47 GMT

←Older revision		Revision as of 23:43, 14 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2glx.png\|left\|200px]]		[[Image:2glx.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2GLX~~ is a 6 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA].	+	[[2glx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_adhaerens Ensifer adhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLX OCA].

	==Reference==		==Reference==
Line 28:		Line 27:
	[[Category: Dambe, T R.]]		[[Category: Dambe, T R.]]
	[[Category: Scheidig, A J.]]		[[Category: Scheidig, A J.]]
-	[[Category: 1,5-anhydro-d-fructose]]	+	[[Category: 5-anhydro-d-fructose]]
-	[[Category: 1,5-anhydro-d-~~mannitol~~]]	+	[[Category: 5-anhydro-d-fructose reductase]]
-	[[Category: ~~Bacterial 1,~~5-anhydro-d-~~fructose reductase~~]]	+	[[Category: 5-anhydro-d-mannitol]]
		+	[[Category: Bacterial 1]]
		+	[[Category: Oxidoreductase]]
	[[Category: Rossmann-fold]]		[[Category: Rossmann-fold]]
	[[Category: Sugar metabolism]]		[[Category: Sugar metabolism]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:35:25 2009''