1t7l - Revision history

OCA at 08:38, 1 May 2024

OCA — Wed, 01 May 2024 08:38:38 GMT

←Older revision		Revision as of 08:38, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='1t7l' size='340' side='right'caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1t7l' size='340' side='right'caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_43589 Atcc 43589~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1T7L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7L FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MRY:MESO~~-~~ERYTHRITOL'>MRY</scene>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~2336 ATCC 43589])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </~~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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [https://pdbe.org/1t7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [https://www.ebi.ac.uk/pdbsum/1t7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7l 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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [~~http~~://pdbe.org/1t7l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1t7l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7l ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/METE_THEMA METE_THEMA]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation (By similarity).	+	[https://www.uniprot.org/uniprot/METE_THEMA METE_THEMA] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t7l 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=1t7l ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L-homocysteine (Hcy) without using an intermediate methyl carrier. Although MetE displays no detectable sequence homology with cobalamin-dependent methionine synthase (MetH), both enzymes require zinc for activation and binding of Hcy. Crystallographic analyses of MetE from T. maritima reveal an unusual dual-barrel structure in which the active site lies between the tops of the two (betaalpha)(8) barrels. The fold of the N-terminal barrel confirms that it has evolved from the C-terminal polypeptide by gene duplication; comparisons of the barrels provide an intriguing example of homologous domain evolution in which binding sites are obliterated. The C-terminal barrel incorporates the zinc ion that binds and activates Hcy. The zinc-binding site in MetE is distinguished from the (Cys)(3)Zn site in the related enzymes, MetH and betaine-homocysteine methyltransferase, by its position in the barrel and by the metal ligands, which are histidine, cysteine, glutamate, and cysteine in the resting form of MetE. Hcy associates at the face of the metal opposite glutamate, which moves away from the zinc in the binary E.Hcy complex. The folate substrate is not intimately associated with the N-terminal barrel; instead, elements from both barrels contribute binding determinants in a binary complex in which the folate substrate is incorrectly oriented for methyl transfer. Atypical locations of the Hcy and folate sites in the C-terminal barrel presumably permit direct interaction of the substrates in a ternary complex. Structures of the binary substrate complexes imply that rearrangement of folate, perhaps accompanied by domain rearrangement, must occur before formation of a ternary complex that is competent for methyl transfer.

-	Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.,Pejchal R, Ludwig ML PLoS Biol. 2005 Feb;3(2):e31. Epub 2004 Dec 28. PMID:15630480<ref>PMID:15630480</ref>	+	==See Also==
-		+	*[[Methionine synthase 3D structures\|Methionine synthase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 1t7l" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
-	[[Category: Atcc 43589]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Ludwig, M L~~]]	+	[[Category: Thermotoga maritima]]
-	[[Category: ~~Pejchal, R~~]]	+	[[Category: Ludwig ML]]
-	[[Category: ~~Homocysteine]]~~	+	[[Category: Pejchal R]]
-	~~[[Category: Methyltetrahydrofolate]]~~	+
-	~~[[Category: Tim barrel]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Zinc~~]]	+

OCA at 11:44, 24 December 2020

OCA — Thu, 24 Dec 2020 11:44:44 GMT

←Older revision		Revision as of 11:44, 24 December 2020
Line 1:		Line 1:

	==Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima==		==Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima==
-	<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1t7l' size='340' side='right'caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1T7L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T7L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://pdbe.org/1t7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7l 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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://pdbe.org/1t7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7l_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7l_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 36:		Line 36:
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Atcc 43589]]		[[Category: Atcc 43589]]
		+	[[Category: Large Structures]]
	[[Category: Ludwig, M L]]		[[Category: Ludwig, M L]]
	[[Category: Pejchal, R]]		[[Category: Pejchal, R]]

OCA at 12:43, 12 October 2017

OCA — Thu, 12 Oct 2017 12:43:28 GMT

←Older revision		Revision as of 12:43, 12 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima==		==Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima==
	<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://pdbe.org/1t7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l 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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://pdbe.org/1t7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 41:		Line 42:
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
	[[Category: Transferase]]		[[Category: Transferase]]
		+	[[Category: Zinc]]

OCA at 02:25, 9 February 2016

OCA — Tue, 09 Feb 2016 02:25:06 GMT

←Older revision		Revision as of 02:25, 9 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=1t7l ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:41, 10 September 2015

OCA — Thu, 10 Sep 2015 17:41:46 GMT

←Older revision		Revision as of 17:41, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermotoga_maritima Thermotoga maritima~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7L FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ~~Thermotoga maritima~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l 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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://pdbe.org/1t7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1t7l" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
-	[[Category: ~~Thermotoga maritima~~]]	+	[[Category: Atcc 43589]]
	[[Category: Ludwig, M L]]		[[Category: Ludwig, M L]]
	[[Category: Pejchal, R]]		[[Category: Pejchal, R]]

OCA at 03:45, 25 December 2014

OCA — Thu, 25 Dec 2014 03:45:54 GMT

←Older revision		Revision as of 03:45, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7L FirstGlance]. <br>		<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7L FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l 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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/METE_THEMA METE_THEMA]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
-	[[Category: Ludwig, M L.]]	+	[[Category: Ludwig, M L]]
-	[[Category: Pejchal, R.]]	+	[[Category: Pejchal, R]]
	[[Category: Homocysteine]]		[[Category: Homocysteine]]
	[[Category: Methyltetrahydrofolate]]		[[Category: Methyltetrahydrofolate]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 19:26, 29 September 2014

OCA — Mon, 29 Sep 2014 19:26:01 GMT

←Older revision		Revision as of 19:26, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1t7l.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima==
		+	<StructureSection load='1t7l' size='340' side='right' caption='[[1t7l]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7L FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRY:MESO-ERYTHRITOL'>MRY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">METE, TM1286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </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=1t7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7l RCSB], [http://www.ebi.ac.uk/pdbsum/1t7l 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/t7/1t7l_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 ==
		+	Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L-homocysteine (Hcy) without using an intermediate methyl carrier. Although MetE displays no detectable sequence homology with cobalamin-dependent methionine synthase (MetH), both enzymes require zinc for activation and binding of Hcy. Crystallographic analyses of MetE from T. maritima reveal an unusual dual-barrel structure in which the active site lies between the tops of the two (betaalpha)(8) barrels. The fold of the N-terminal barrel confirms that it has evolved from the C-terminal polypeptide by gene duplication; comparisons of the barrels provide an intriguing example of homologous domain evolution in which binding sites are obliterated. The C-terminal barrel incorporates the zinc ion that binds and activates Hcy. The zinc-binding site in MetE is distinguished from the (Cys)(3)Zn site in the related enzymes, MetH and betaine-homocysteine methyltransferase, by its position in the barrel and by the metal ligands, which are histidine, cysteine, glutamate, and cysteine in the resting form of MetE. Hcy associates at the face of the metal opposite glutamate, which moves away from the zinc in the binary E.Hcy complex. The folate substrate is not intimately associated with the N-terminal barrel; instead, elements from both barrels contribute binding determinants in a binary complex in which the folate substrate is incorrectly oriented for methyl transfer. Atypical locations of the Hcy and folate sites in the C-terminal barrel presumably permit direct interaction of the substrates in a ternary complex. Structures of the binary substrate complexes imply that rearrangement of folate, perhaps accompanied by domain rearrangement, must occur before formation of a ternary complex that is competent for methyl transfer.

-	~~{{STRUCTURE_1t7l\| PDB=1t7l \| SCENE= }}~~	+	Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.,Pejchal R, Ludwig ML PLoS Biol. 2005 Feb;3(2):e31. Epub 2004 Dec 28. PMID:15630480<ref>PMID:15630480</ref>

-	~~===Crystal Structure~~ of ~~Cobalamin-Independent Methionine Synthase from T~~. ~~maritima===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15630480}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1t7l]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015630480<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]

OCA: Protected "1t7l" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 12:29:39 GMT

Protected "1t7l" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:29, 5 January 2013

OCA at 12:29, 5 January 2013

OCA — Sat, 05 Jan 2013 12:29:36 GMT

←Older revision		Revision as of 12:29, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1t7l.png\|left\|200px]]		[[Image:1t7l.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1t7l", 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_1t7l\| PDB=1t7l \| SCENE= }}		{{STRUCTURE_1t7l\| PDB=1t7l \| SCENE= }}

	===Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima===		===Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15630480}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15630480 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15630480}}		{{ABSTRACT_PUBMED_15630480}}

	==About this Structure==		==About this Structure==
-	~~1T7L~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA].	+	[[1t7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15630480~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015630480</ref><references group="xtra"/>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
Line 31:		Line 19:
	[[Category: Methyltetrahydrofolate]]		[[Category: Methyltetrahydrofolate]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
-	[[Category: ~~Zinc~~]]	+	[[Category: Transferase]]
-		+
-	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:42:44 2009''~~	+

OCA at 03:42, 17 February 2009

OCA — Tue, 17 Feb 2009 03:42:45 GMT

←Older revision		Revision as of 03:42, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1T7L is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA].	+	1T7L is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7L OCA].

	==Reference==		==Reference==
-	~~Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication., Pejchal R, Ludwig ML, PLoS Biol. 2005 Feb;3(2):e31. Epub 2004 Dec 28.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15630480 15630480]~~	+	<ref group="xtra">PMID:15630480</ref><references group="xtra"/>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
-	[[Category: Single protein]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
	[[Category: Ludwig, M L.]]		[[Category: Ludwig, M L.]]
Line 34:		Line 33:
	[[Category: Zinc]]		[[Category: Zinc]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 09~~:06:~~45 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:42:44 2009''