1fa7 - Revision history

OCA at 07:12, 7 February 2024

OCA — Wed, 07 Feb 2024 07:12:31 GMT

←Older revision		Revision as of 07:12, 7 February 2024
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	<StructureSection load='1fa7' size='340' side='right'caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1fa7' size='340' side='right'caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CD:CADMIUM+ION'>CD</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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5]~~ </~~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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [https://pdbe.org/1fa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [https://pdbe.org/1fa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>	+	[https://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>
	== 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=1fa7 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=1fa7 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The metalloenzyme glyoxalase I (GlxI) converts the nonenzymatically produced hemimercaptal of cytotoxic methylglyoxal and glutathione to nontoxic S-D-lactoylglutathione. Human GlxI, for which the structure is known, is active in the presence of Zn(2+). Unexpectedly, the Escherichia coli enzyme is inactive in the presence of Zn(2+) and is maximally active with Ni(2+). To understand this difference in metal activation and also to obtain a representative of the bacterial enzymes, the structure of E. coli Ni(2+)-GlxI has been determined. Structures have also been determined for the apo enzyme as well as complexes with Co(2+), Cd(2+), and Zn(2+). It is found that each of the protein-metal complexes that is catalytically active has octahedral geometry. This includes the complexes of the E. coli enzyme with Ni(2+), Co(2+), and Cd(2+), as well as the structures reported for the human Zn(2+) enzyme. Conversely, the complex of the E. coli enzyme with Zn(2+) has trigonal bipyramidal coordination and is inactive. This mode of coordination includes four protein ligands plus a single water molecule. In contrast, the coordination in the active forms of the enzyme includes two water molecules bound to the metal ion, suggesting that this may be a key feature of the catalytic mechanism. A comparison of the human and E. coli enzymes suggests that there are differences between the active sites that might be exploited for therapeutic use.
-
-	Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.,He MM, Clugston SL, Honek JF, Matthews BW Biochemistry. 2000 Aug 1;39(30):8719-27. PMID:10913283<ref>PMID:10913283</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895]]~~	+	[[Category: Escherichia coli]]
-	~~[[Category: Lactoylglutathione lyase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Clugston~~, S L~~]]	+	[[Category: Clugston SL]]
-	[[Category: He~~, M M~~]]	+	[[Category: He MM]]
-	[[Category: Honek~~, J F~~]]	+	[[Category: Honek JF]]
-	[[Category: Matthews~~, B W]]~~	+	[[Category: Matthews BW]]
-	~~[[Category: Beta-alpha-beta-beta-beta motif]]~~	+
-	~~[[Category: Homodimer]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 09:48, 21 July 2021

OCA — Wed, 21 Jul 2021 09:48:27 GMT

←Older revision		Revision as of 09:48, 21 July 2021
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	<StructureSection load='1fa7' size='340' side='right'caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1fa7' size='340' side='right'caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [~~http~~://pdbe.org/1fa7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [https://pdbe.org/1fa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>	+	[[https://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:52, 16 October 2019

OCA — Wed, 16 Oct 2019 10:52:29 GMT

←Older revision		Revision as of 10:52, 16 October 2019
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	==CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==		==CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==
-	<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1fa7' size='340' side='right'caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glyoxalase 3D structures\|Glyoxalase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
	[[Category: Lactoylglutathione lyase]]		[[Category: Lactoylglutathione lyase]]
		+	[[Category: Large Structures]]
	[[Category: Clugston, S L]]		[[Category: Clugston, S L]]
	[[Category: He, M M]]		[[Category: He, M M]]

OCA at 09:31, 27 December 2017

OCA — Wed, 27 Dec 2017 09:31:09 GMT

←Older revision		Revision as of 09:31, 27 December 2017
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		+
	==CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==		==CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==
	<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://pdbe.org/1fa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://pdbe.org/1fa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fa7_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fa7_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 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glyoxalase\|Glyoxalase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:36, 8 February 2016

OCA — Mon, 08 Feb 2016 07:36:40 GMT

←Older revision		Revision as of 07:36, 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=1fa7 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:19, 10 September 2015

OCA — Thu, 10 Sep 2015 09:19:00 GMT

←Older revision		Revision as of 09:19, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://pdbe.org/1fa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1fa7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Lactoylglutathione lyase]]		[[Category: Lactoylglutathione lyase]]
	[[Category: Clugston, S L]]		[[Category: Clugston, S L]]

OCA at 21:41, 24 December 2014

OCA — Wed, 24 Dec 2014 21:41:26 GMT

←Older revision		Revision as of 21:41, 24 December 2014
Line 8:		Line 8:
	<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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 00:21, 23 December 2014

OCA — Tue, 23 Dec 2014 00:21:05 GMT

←Older revision		Revision as of 00:21, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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 35:		Line 35:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Lactoylglutathione lyase]]		[[Category: Lactoylglutathione lyase]]
-	[[Category: Clugston, S L.]]	+	[[Category: Clugston, S L]]
-	[[Category: He, M M.]]	+	[[Category: He, M M]]
-	[[Category: Honek, J F.]]	+	[[Category: Honek, J F]]
-	[[Category: Matthews, B W.]]	+	[[Category: Matthews, B W]]
	[[Category: Beta-alpha-beta-beta-beta motif]]		[[Category: Beta-alpha-beta-beta-beta motif]]
	[[Category: Homodimer]]		[[Category: Homodimer]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 14:08, 28 September 2014

OCA — Sun, 28 Sep 2014 14:08:14 GMT

←Older revision		Revision as of 14:08, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fa7.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==
		+	<StructureSection load='1fa7' size='340' side='right' caption='[[1fa7]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fa7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA7 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9z\|1f9z]], [[1fa5\|1fa5]], [[1fa6\|1fa6]], [[1fa8\|1fa8]], [[1fro\|1fro]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa7 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/fa/1fa7_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 ==
		+	The metalloenzyme glyoxalase I (GlxI) converts the nonenzymatically produced hemimercaptal of cytotoxic methylglyoxal and glutathione to nontoxic S-D-lactoylglutathione. Human GlxI, for which the structure is known, is active in the presence of Zn(2+). Unexpectedly, the Escherichia coli enzyme is inactive in the presence of Zn(2+) and is maximally active with Ni(2+). To understand this difference in metal activation and also to obtain a representative of the bacterial enzymes, the structure of E. coli Ni(2+)-GlxI has been determined. Structures have also been determined for the apo enzyme as well as complexes with Co(2+), Cd(2+), and Zn(2+). It is found that each of the protein-metal complexes that is catalytically active has octahedral geometry. This includes the complexes of the E. coli enzyme with Ni(2+), Co(2+), and Cd(2+), as well as the structures reported for the human Zn(2+) enzyme. Conversely, the complex of the E. coli enzyme with Zn(2+) has trigonal bipyramidal coordination and is inactive. This mode of coordination includes four protein ligands plus a single water molecule. In contrast, the coordination in the active forms of the enzyme includes two water molecules bound to the metal ion, suggesting that this may be a key feature of the catalytic mechanism. A comparison of the human and E. coli enzymes suggests that there are differences between the active sites that might be exploited for therapeutic use.

-	~~{{STRUCTURE_1fa7\| PDB=1fa7 \| SCENE= }}~~	+	Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.,He MM, Clugston SL, Honek JF, Matthews BW Biochemistry. 2000 Aug 1;39(30):8719-27. PMID:10913283<ref>PMID:10913283</ref>

-	~~===CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10913283}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1fa7]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1FA7 OCA].~~	+

	==See Also==		==See Also==
	*[[Glyoxalase\|Glyoxalase]]		*[[Glyoxalase\|Glyoxalase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:010913283<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Lactoylglutathione lyase]]		[[Category: Lactoylglutathione lyase]]

OCA: Protected "1fa7" [edit=sysop:move=sysop]

OCA — Sat, 20 Oct 2012 09:25:06 GMT

Protected "1fa7" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:25, 20 October 2012