1lt8 - Revision history

OCA at 07:35, 14 February 2024

OCA — Wed, 14 Feb 2024 07:35:55 GMT

←Older revision		Revision as of 07:35, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1lt8' size='340' side='right'caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1lt8' size='340' side='right'caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CBH:S~~-~~(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>~~, ~~<scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.05Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1lt7\|1lt7]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </~~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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [https://pdbe.org/1lt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [https://www.ebi.ac.uk/pdbsum/1lt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt8 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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [https://pdbe.org/1lt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [https://www.ebi.ac.uk/pdbsum/1lt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN]] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.	+	[https://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
	== 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=1lt8 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=1lt8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family.
-
-	Betaine-homocysteine methyltransferase: zinc in a distorted barrel.,Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML Structure. 2002 Sep;10(9):1159-71. PMID:12220488<ref>PMID:12220488</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1lt8" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Betaine--homocysteine S-methyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Castro, C]]	+	[[Category: Castro C]]
-	[[Category: Evans~~, J C~~]]	+	[[Category: Evans JC]]
-	[[Category: Garrow~~, T A~~]]	+	[[Category: Garrow TA]]
-	[[Category: Huddler~~, D P~~]]	+	[[Category: Huddler DP]]
-	[[Category: Jiracek, J]]	+	[[Category: Jiracek J]]
-	[[Category: Ludwig~~, M L~~]]	+	[[Category: Ludwig ML]]
-	[[Category: Millian~~, N S]]~~	+	[[Category: Millian NS]]
-	~~[[Category: Homocysteine metabolism]]~~	+
-	~~[[Category: Homocysteinemia]]~~	+
-	~~[[Category: Thiol alkyl transfer]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Zinc~~]]	+

OCA at 06:48, 18 August 2021

OCA — Wed, 18 Aug 2021 06:48:54 GMT

←Older revision		Revision as of 06:48, 18 August 2021
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	<StructureSection load='1lt8' size='340' side='right'caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1lt8' size='340' side='right'caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lt7\|1lt7]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [~~http~~://pdbe.org/1lt8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1lt8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt8 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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [https://pdbe.org/1lt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [https://www.ebi.ac.uk/pdbsum/1lt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN]] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.	+	[[https://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN]] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:12, 13 November 2019

OCA — Wed, 13 Nov 2019 12:12:40 GMT

←Older revision		Revision as of 12:12, 13 November 2019
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	==Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine==		==Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine==
-	<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>	+	<StructureSection load='1lt8' size='340' side='right'caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
Line 36:		Line 36:
	[[Category: Betaine--homocysteine S-methyltransferase]]		[[Category: Betaine--homocysteine S-methyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Castro, C]]		[[Category: Castro, C]]
	[[Category: Evans, J C]]		[[Category: Evans, J C]]

OCA at 07:48, 31 January 2018

OCA — Wed, 31 Jan 2018 07:48:51 GMT

←Older revision		Revision as of 07:48, 31 January 2018
Line 1:		Line 1:
		+
	==Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine==		==Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine==
	<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://pdbe.org/1lt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://pdbe.org/1lt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt8 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/lt/1lt8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lt8_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 46:		Line 47:
	[[Category: Thiol alkyl transfer]]		[[Category: Thiol alkyl transfer]]
	[[Category: Transferase]]		[[Category: Transferase]]
		+	[[Category: Zinc]]

OCA at 11:08, 8 February 2016

OCA — Mon, 08 Feb 2016 11:08:05 GMT

←Older revision		Revision as of 11:08, 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=1lt8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 10:55, 10 September 2015

OCA — Thu, 10 Sep 2015 10:55:03 GMT

←Older revision		Revision as of 10:55, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://pdbe.org/1lt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 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 1lt8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Betaine--homocysteine S-methyltransferase]]		[[Category: Betaine--homocysteine S-methyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Castro, C]]		[[Category: Castro, C]]
	[[Category: Evans, J C]]		[[Category: Evans, J C]]

OCA at 22:52, 24 December 2014

OCA — Wed, 24 Dec 2014 22:52:35 GMT

←Older revision		Revision as of 22:52, 24 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN]] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Betaine--homocysteine S-methyltransferase]]		[[Category: Betaine--homocysteine S-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Castro, C.]]	+	[[Category: Castro, C]]
-	[[Category: Evans, J C.]]	+	[[Category: Evans, J C]]
-	[[Category: Garrow, T A.]]	+	[[Category: Garrow, T A]]
-	[[Category: Huddler, D P.]]	+	[[Category: Huddler, D P]]
-	[[Category: Jiracek, J.]]	+	[[Category: Jiracek, J]]
-	[[Category: Ludwig, M L.]]	+	[[Category: Ludwig, M L]]
-	[[Category: Millian, N S.]]	+	[[Category: Millian, N S]]
	[[Category: Homocysteine metabolism]]		[[Category: Homocysteine metabolism]]
	[[Category: Homocysteinemia]]		[[Category: Homocysteinemia]]
	[[Category: Thiol alkyl transfer]]		[[Category: Thiol alkyl transfer]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:45, 28 September 2014

OCA — Sun, 28 Sep 2014 13:45:12 GMT

←Older revision		Revision as of 13:45, 28 September 2014
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-	[[~~Image:~~1lt8.~~png~~\|~~left~~\|200px]]	+	==Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine==
		+	<StructureSection load='1lt8' size='340' side='right' caption='[[1lt8]], [[Resolution\|resolution]] 2.05Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LT8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lt7\|1lt7]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] </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=1lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lt8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lt8 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/lt/1lt8_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 ==
		+	Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family.

-	~~{{STRUCTURE_1lt8\| PDB=1lt8 \| SCENE= }}~~	+	Betaine-homocysteine methyltransferase: zinc in a distorted barrel.,Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML Structure. 2002 Sep;10(9):1159-71. PMID:12220488<ref>PMID:12220488</ref>

-	~~===Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12220488}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1lt8]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:012220488<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Betaine--homocysteine S-methyltransferase]]		[[Category: Betaine--homocysteine S-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "1lt8" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 20:48:57 GMT

Protected "1lt8" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:48, 5 December 2012

OCA at 20:48, 5 December 2012

OCA — Wed, 05 Dec 2012 20:48:53 GMT

←Older revision		Revision as of 20:48, 5 December 2012
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-	{{Seed}}
	[[Image:1lt8.png\|left\|200px]]		[[Image:1lt8.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1lt8\| PDB=1lt8 \| SCENE= }}		{{STRUCTURE_1lt8\| PDB=1lt8 \| SCENE= }}

	===Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine===		===Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12220488}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12220488 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_12220488}}		{{ABSTRACT_PUBMED_12220488}}

	==About this Structure==		==About this Structure==
-	~~1LT8~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA].	+	[[1lt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT8 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12220488~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012220488</ref><references group="xtra"/>
	[[Category: Betaine--homocysteine S-methyltransferase]]		[[Category: Betaine--homocysteine S-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 37:		Line 25:
	[[Category: Thiol alkyl transfer]]		[[Category: Thiol alkyl transfer]]
	[[Category: Transferase]]		[[Category: Transferase]]
-	[[Category: Zinc]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:32:31 2009''