1wze - Revision history

OCA at 08:02, 25 October 2023

OCA — Wed, 25 Oct 2023 08:02:41 GMT

←Older revision		Revision as of 08:02, 25 October 2023
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	<StructureSection load='1wze' size='340' side='right'caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1wze' size='340' side='right'caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NAD:NICOTINAMIDE~~-~~ADENINE-DINUCLEOTIDE'>NAD</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]] 2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>mdh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~274~~ "~~Flavobacterium thermophilum~~" ~~Yoshida and Oshima 1971])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37]~~ </~~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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [https://pdbe.org/1wze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [https://www.ebi.ac.uk/pdbsum/1wze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze 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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [https://pdbe.org/1wze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [https://www.ebi.ac.uk/pdbsum/1wze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MDH_THETH MDH_THETH]] Catalyzes the reversible oxidation of malate to oxaloacetate.	+	[https://www.uniprot.org/uniprot/MDH_THETH MDH_THETH] Catalyzes the reversible oxidation of malate to oxaloacetate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1wze 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=1wze ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	A binary complex of malate dehydrogenase from the thermophilic bacterium Thermus flavus (tMDH) with NADH has been crystallized from poly(ethylene glycol) 3500, pH 8.5, yielding diffraction-quality crystals in space group P2(1)2(1)2(1). The structure was solved at 1.9-A resolution using molecular replacement and refined to an R factor of 15.8% with good geometry. The primary sequence of tMDH is 55% identical to that of cytoplasmic malate dehydrogenase (cMDH) [Birktoft, J. J., Rhodes, G., & Banaszak, L. J. (1989) Biochemistry 28, 6065-6081], and overall their three-dimensional structures are very similar. Like cMDH, tMDH crystallized as a dimer with one coenzyme bound per subunit. The coenzyme binds in the extended conformation, and most of the interactions with enzyme are similar to those in cMDH. In tMDH, small local conformational changes are caused by the replacement of a glutamic acid for the aspartic acid involved in hydrogen bonding to the adenine ribose of NADH. Comparison of tMDH with cMDH reveals that both tMDH subunits more closely resemble the B subunit of cMDH which therefore is the more likely representative of the solution conformation. While cMDH is inactivated at temperatures above about 50 degrees C, tMDH is fully active at 90 degrees C. On the basis of the X-ray crystal structure, a number of factors have been identified which are likely to contribute to the relative thermostability of tMDH compared to cMDH. The most striking of the differences involves the introduction of four ion pairs per monomer. All of these ion pairs are solvent-accessible. Three of these ion pairs are located in the dimer interface, Glu27-Lys31, Glu57-Lys168, and Glu57-Arg229, and one ion pair, Glu275-Arg149, is at the domain interface within each subunit. Additionally, we observe incorporation of additional alanines into alpha-helices of tMDH and, in one instance, incorporation of an aspartate that functions as a counterchange to an alpha-helix dipole. The possible contributions of these and other factors to protein thermostability in tMDH are discussed.
-
-	Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.,Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ Biochemistry. 1993 Apr 20;32(15):3913-22. PMID:8471603<ref>PMID:8471603</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Malate Dehydrogenase 3D structures\|Malate Dehydrogenase 3D structures]]		*[[Malate Dehydrogenase 3D structures\|Malate Dehydrogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Malate dehydrogenase~~]]	+	[[Category: Thermus thermophilus]]
-	[[Category: Fushinobu, S]]	+	[[Category: Fushinobu S]]
-	[[Category: Kuzuyama, T]]	+	[[Category: Kuzuyama T]]
-	[[Category: Nishiyama, M]]	+	[[Category: Nishiyama M]]
-	[[Category: Tomita, T]]	+	[[Category: Tomita T]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Protein-nadh complex]]~~	+
-	~~[[Category: Seven amino acid residues mutant~~]]	+

OCA at 06:37, 10 November 2021

OCA — Wed, 10 Nov 2021 06:37:53 GMT

OCA at 09:32, 6 January 2021

OCA — Wed, 06 Jan 2021 09:32:59 GMT

←Older revision		Revision as of 09:32, 6 January 2021
Line 1:		Line 1:

	==Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus==		==Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus==
-	<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1wze' size='340' side='right'caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1WZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://pdbe.org/1wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://pdbe.org/1wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wze_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wze_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Malate Dehydrogenase 3D structures\|Malate Dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]		[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
		+	[[Category: Large Structures]]
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]

OCA at 07:01, 29 November 2017

OCA — Wed, 29 Nov 2017 07:01:15 GMT

←Older revision		Revision as of 07:01, 29 November 2017
Line 1:		Line 1:
		+
	==Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus==		==Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus==
	<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://pdbe.org/1wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze 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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://pdbe.org/1wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Malate dehydrogenase\|Malate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:48, 9 February 2016

OCA — Tue, 09 Feb 2016 10:48:00 GMT

←Older revision		Revision as of 10:48, 9 February 2016
Line 19:		Line 19:
	<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=1wze ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:32, 10 September 2015

OCA — Thu, 10 Sep 2015 21:32:36 GMT

←Older revision		Revision as of 21:32, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermus_thermophilus Thermus thermophilus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 ~~Thermus thermophilus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze 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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://pdbe.org/1wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1wze" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
-	[[Category: Thermus thermophilus]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]
	[[Category: Kuzuyama, T]]		[[Category: Kuzuyama, T]]

OCA at 06:22, 25 December 2014

OCA — Thu, 25 Dec 2014 06:22:23 GMT

←Older revision		Revision as of 06:22, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze 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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MDH_THETH MDH_THETH]] Catalyzes the reversible oxidation of malate to oxaloacetate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
-	[[Category: Fushinobu, S.]]	+	[[Category: Fushinobu, S]]
-	[[Category: Kuzuyama, T.]]	+	[[Category: Kuzuyama, T]]
-	[[Category: Nishiyama, M.]]	+	[[Category: Nishiyama, M]]
-	[[Category: Tomita, T.]]	+	[[Category: Tomita, T]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Protein-nadh complex]]		[[Category: Protein-nadh complex]]
	[[Category: Seven amino acid residues mutant]]		[[Category: Seven amino acid residues mutant]]

OCA at 05:16, 3 October 2014

OCA — Fri, 03 Oct 2014 05:16:36 GMT

←Older revision		Revision as of 05:16, 3 October 2014
Line 1:		Line 1:
-	[[~~Image:~~1wze.~~png~~\|~~left~~\|200px]]	+	==Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus==
		+	<StructureSection load='1wze' size='340' side='right' caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [http://www.ebi.ac.uk/pdbsum/1wze 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/wz/1wze_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 ==
		+	A binary complex of malate dehydrogenase from the thermophilic bacterium Thermus flavus (tMDH) with NADH has been crystallized from poly(ethylene glycol) 3500, pH 8.5, yielding diffraction-quality crystals in space group P2(1)2(1)2(1). The structure was solved at 1.9-A resolution using molecular replacement and refined to an R factor of 15.8% with good geometry. The primary sequence of tMDH is 55% identical to that of cytoplasmic malate dehydrogenase (cMDH) [Birktoft, J. J., Rhodes, G., & Banaszak, L. J. (1989) Biochemistry 28, 6065-6081], and overall their three-dimensional structures are very similar. Like cMDH, tMDH crystallized as a dimer with one coenzyme bound per subunit. The coenzyme binds in the extended conformation, and most of the interactions with enzyme are similar to those in cMDH. In tMDH, small local conformational changes are caused by the replacement of a glutamic acid for the aspartic acid involved in hydrogen bonding to the adenine ribose of NADH. Comparison of tMDH with cMDH reveals that both tMDH subunits more closely resemble the B subunit of cMDH which therefore is the more likely representative of the solution conformation. While cMDH is inactivated at temperatures above about 50 degrees C, tMDH is fully active at 90 degrees C. On the basis of the X-ray crystal structure, a number of factors have been identified which are likely to contribute to the relative thermostability of tMDH compared to cMDH. The most striking of the differences involves the introduction of four ion pairs per monomer. All of these ion pairs are solvent-accessible. Three of these ion pairs are located in the dimer interface, Glu27-Lys31, Glu57-Lys168, and Glu57-Arg229, and one ion pair, Glu275-Arg149, is at the domain interface within each subunit. Additionally, we observe incorporation of additional alanines into alpha-helices of tMDH and, in one instance, incorporation of an aspartate that functions as a counterchange to an alpha-helix dipole. The possible contributions of these and other factors to protein thermostability in tMDH are discussed.

-	~~{{STRUCTURE_1wze\| PDB=1wze \| SCENE= }}~~	+	Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.,Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ Biochemistry. 1993 Apr 20;32(15):3913-22. PMID:8471603<ref>PMID:8471603</ref>

-	~~===Structural basis for alteration~~ of ~~cofactor specificity of Malate dehydrogenase from Thermus flavus===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8471603}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1wze]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermus_thermophilus Thermus thermophilus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA].~~	+

	==See Also==		==See Also==
-	*[[Johnson sandbox 1\|Johnson sandbox 1]]
	*[[Malate dehydrogenase\|Malate dehydrogenase]]		*[[Malate dehydrogenase\|Malate dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008471603<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]

OCA at 13:37, 20 October 2012

OCA — Sat, 20 Oct 2012 13:37:54 GMT

←Older revision		Revision as of 13:37, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1wze]] is a 2 chain structure ~~of [[Johnson sandbox 1]] and [[Malate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA].	+	[[1wze]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA].

	==See Also==		==See Also==
Line 15:		Line 15:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008471603~~</ref><ref group="xtra">PMID:001920425</ref><ref group="xtra">PMID:002775751</ref><ref group="xtra">PMID:003771528</ref><ref group="xtra">PMID:006848515~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008471603</ref><references group="xtra"/>
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]

OCA at 12:35, 26 July 2012

OCA — Thu, 26 Jul 2012 12:35:18 GMT

←Older revision		Revision as of 12:35, 26 July 2012
Line 1:		Line 1:
	[[Image:1wze.png\|left\|200px]]		[[Image:1wze.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1wze", 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_1wze\| PDB=1wze \| SCENE= }}		{{STRUCTURE_1wze\| PDB=1wze \| SCENE= }}

	===Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus===		===Structural basis for alteration of cofactor specificity of Malate dehydrogenase from Thermus flavus===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8471603}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8471603 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8471603}}		{{ABSTRACT_PUBMED_8471603}}

	==About this Structure==		==About this Structure==
-	[[1wze]] is a 2 chain structure of [[Malate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA].	+	[[1wze]] is a 2 chain structure of [[Johnson sandbox 1]] and [[Malate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA].

	==See Also==		==See Also==
-	*[[Malate dehydrogenase]]	+	*[[Johnson sandbox 1\|Johnson sandbox 1]]
		+	*[[Malate dehydrogenase\|Malate dehydrogenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8471603~~</ref><ref group="xtra">PMID:~~1920425~~</ref><ref group="xtra">PMID:~~2775751~~</ref><ref group="xtra">PMID:~~3771528~~</ref><ref group="xtra">PMID:~~6848515~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008471603</ref><ref group="xtra">PMID:001920425</ref><ref group="xtra">PMID:002775751</ref><ref group="xtra">PMID:003771528</ref><ref group="xtra">PMID:006848515</ref><references group="xtra"/>
	[[Category: Malate dehydrogenase]]		[[Category: Malate dehydrogenase]]
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]

←Older revision		Revision as of 06:37, 10 November 2021
Line 3:		Line 3:
	<StructureSection load='1wze' size='340' side='right'caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1wze' size='340' side='right'caption='[[1wze]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1WZE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bmd\|1bmd]], [[1y7t\|1y7t]], [[1wzi\|1wzi]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mdh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [~~http~~://pdbe.org/1wze PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1wze PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze 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=1wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wze OCA], [https://pdbe.org/1wze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wze RCSB], [https://www.ebi.ac.uk/pdbsum/1wze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wze ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MDH_THETH MDH_THETH]] Catalyzes the reversible oxidation of malate to oxaloacetate.	+	[[https://www.uniprot.org/uniprot/MDH_THETH MDH_THETH]] Catalyzes the reversible oxidation of malate to oxaloacetate.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]