1u22 - Revision history

OCA at 06:16, 3 April 2024

OCA — Wed, 03 Apr 2024 06:16:01 GMT

←Older revision		Revision as of 06:16, 3 April 2024
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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=1u22 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=1u22 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 synthesis of methionine by a direct transfer of the methyl group of N5-methyltetrahydrofolate (CH3-H2PteGlun) to the sulfur atom of homocysteine (Hcy). We report here the first crystal structure of this metalloenzyme under different forms, free or complexed with the Hcy and folate substrates. The Arabidopsis thaliana MetE (AtMetE) crystals reveal a monomeric structure built by two (betaalpha)8 barrels making a deep groove at their interface. The active site is located at the surface of the C-terminal domain, facing the large interdomain cleft. Inside the active site, His647, Cys649, and Cys733 are involved in zinc coordination, whereas Asp605, Ile437, and Ser439 interact with Hcy. Opposite the zinc/Hcy binding site, a cationic loop (residues 507-529) belonging to the C-terminal domain anchors the first glutamyl residue of CH3-H4PteGlu5. The pterin moiety of CH3-H4PteGlu5 is stacked with Trp567, enabling the N5-methyl group to protrude in the direction of the zinc atom. These data suggest a structural role of the N-terminal domain of AtMetE in the stabilization of loop 507-529 and in the interaction with the poly-glutamate chain of CH3-H4PteGlun. Comparison of AtMetE structures reveals that the addition of Hcy does not lead to a direct coordination of the sulfur atom with zinc but to a reorganization of the zinc binding site with a stronger coordination to Cys649, Cys733, and a water molecule.
-
-	Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate.,Ferrer JL, Ravanel S, Robert M, Dumas R J Biol Chem. 2004 Oct 22;279(43):44235-8. Epub 2004 Aug 23. PMID:15326182<ref>PMID:15326182</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1u22" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 06:37, 23 August 2023

OCA — Wed, 23 Aug 2023 06:37:02 GMT

←Older revision		Revision as of 06:37, 23 August 2023
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	<StructureSection load='1u22' size='340' side='right'caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='1u22' size='340' side='right'caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Arath Arath~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1U22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HCS:2~~-~~AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>~~, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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]] 2.65Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~MSE~~:~~SELENOMETHIONINE~~'>~~MSE~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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"><div style~~=~~'overflow~~: ~~auto; max-height: 3em;~~'>~~[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]~~</~~div~~><~~/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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [https://pdbe.org/1u22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [https://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">CIMS~~ (~~[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5~~&id=3702 ARATH])</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~~://proteopedia.org/fgij/fg.htm?mol=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [~~http~~://pdbe.org/1u22 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~METE_ARATH METE_ARATH]~~] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.	+	[https://www.uniprot.org/uniprot/METE1_ARATH METE1_ARATH] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.<ref>PMID:15024005</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1u22" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1u22" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Methionine synthase 3D structures\|Methionine synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]~~	+	[[Category: Arabidopsis thaliana]]
-	~~[[Category: Arath~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dumas, R]]	+	[[Category: Dumas R]]
-	[[Category: Ferrer, J L]]	+	[[Category: Ferrer J-L]]
-	[[Category: Ravanel, S]]	+	[[Category: Ravanel S]]
-	[[Category: Robert, M]]	+	[[Category: Robert M]]
-	~~[[Category: Homocysteine]]~~	+
-	~~[[Category: Methionine]]~~	+
-	~~[[Category: Methyltetrahydrofolate]]~~	+
-	~~[[Category: Synthase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:19, 30 December 2020

OCA — Wed, 30 Dec 2020 07:19:07 GMT

←Older revision		Revision as of 07:19, 30 December 2020
Line 1:		Line 1:

	==A. thaliana cobalamine independent methionine synthase==		==A. thaliana cobalamine independent methionine synthase==
-	<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>	+	<StructureSection load='1u22' size='340' side='right'caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1U22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://pdbe.org/1u22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://pdbe.org/1u22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Arath]]		[[Category: Arath]]
		+	[[Category: Large Structures]]
	[[Category: Dumas, R]]		[[Category: Dumas, R]]
	[[Category: Ferrer, J L]]		[[Category: Ferrer, J L]]

OCA at 08:40, 21 March 2018

OCA — Wed, 21 Mar 2018 08:40:33 GMT

←Older revision		Revision as of 08:40, 21 March 2018
Line 1:		Line 1:
		+
	==A. thaliana cobalamine independent methionine synthase==		==A. thaliana cobalamine independent methionine synthase==
	<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://pdbe.org/1u22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://pdbe.org/1u22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u22_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u2/1u22_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>
	</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=1u22 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:57, 11 September 2015

OCA — Fri, 11 Sep 2015 09:57:05 GMT

←Older revision		Revision as of 09:57, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Arabidopsis_thaliana Arabidopsis thaliana~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ~~Arabidopsis thaliana~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://pdbe.org/1u22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 30:
	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 1u22" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
-	[[Category: ~~Arabidopsis thaliana~~]]	+	[[Category: Arath]]
	[[Category: Dumas, R]]		[[Category: Dumas, R]]
	[[Category: Ferrer, J L]]		[[Category: Ferrer, J L]]

OCA at 14:49, 25 December 2014

OCA — Thu, 25 Dec 2014 14:49:30 GMT

←Older revision		Revision as of 14:49, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U22 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/METE_ARATH METE_ARATH]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
-	[[Category: Dumas, R.]]	+	[[Category: Dumas, R]]
-	[[Category: Ferrer, J L.]]	+	[[Category: Ferrer, J L]]
-	[[Category: Ravanel, S.]]	+	[[Category: Ravanel, S]]
-	[[Category: Robert, M.]]	+	[[Category: Robert, M]]
	[[Category: Homocysteine]]		[[Category: Homocysteine]]
	[[Category: Methionine]]		[[Category: Methionine]]

OCA at 04:15, 3 October 2014

OCA — Fri, 03 Oct 2014 04:15:12 GMT

←Older revision		Revision as of 04:15, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1u22~~\| ~~PDB~~=1u22 \| ~~SCENE~~= }}	+	==A. thaliana cobalamine independent methionine synthase==
-	===A. thaliana ~~cobalamine independent methionine synthase~~===	+	<StructureSection load='1u22' size='340' side='right' caption='[[1u22]], [[Resolution\|resolution]] 2.65Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15326182}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1u1h\|1u1h]], [[1u1u\|1u1u]], [[1u1j\|1u1j]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CIMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [http://www.ebi.ac.uk/pdbsum/1u22 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/u2/1u22_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 synthesis of methionine by a direct transfer of the methyl group of N5-methyltetrahydrofolate (CH3-H2PteGlun) to the sulfur atom of homocysteine (Hcy). We report here the first crystal structure of this metalloenzyme under different forms, free or complexed with the Hcy and folate substrates. The Arabidopsis thaliana MetE (AtMetE) crystals reveal a monomeric structure built by two (betaalpha)8 barrels making a deep groove at their interface. The active site is located at the surface of the C-terminal domain, facing the large interdomain cleft. Inside the active site, His647, Cys649, and Cys733 are involved in zinc coordination, whereas Asp605, Ile437, and Ser439 interact with Hcy. Opposite the zinc/Hcy binding site, a cationic loop (residues 507-529) belonging to the C-terminal domain anchors the first glutamyl residue of CH3-H4PteGlu5. The pterin moiety of CH3-H4PteGlu5 is stacked with Trp567, enabling the N5-methyl group to protrude in the direction of the zinc atom. These data suggest a structural role of the N-terminal domain of AtMetE in the stabilization of loop 507-529 and in the interaction with the poly-glutamate chain of CH3-H4PteGlun. Comparison of AtMetE structures reveals that the addition of Hcy does not lead to a direct coordination of the sulfur atom with zinc but to a reorganization of the zinc binding site with a stronger coordination to Cys649, Cys733, and a water molecule.

-	~~==Function==~~	+	Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate.,Ferrer JL, Ravanel S, Robert M, Dumas R J Biol Chem. 2004 Oct 22;279(43):44235-8. Epub 2004 Aug 23. PMID:15326182<ref>PMID:15326182</ref>
-	~~[[http://www.uniprot.org/uniprot/METE_ARATH METE_ARATH]] Catalyzes the transfer~~ of ~~a methyl group from 5~~-~~methyltetrahydrofolate to homocysteine resulting in~~ methionine ~~formation~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1u22]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:015326182</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]

OCA at 06:45, 2 May 2013

OCA — Thu, 02 May 2013 06:45:21 GMT

←Older revision		Revision as of 06:45, 2 May 2013
Line 1:		Line 1:
-	[[Image:1u22.png\|left\|200px]]
-
	{{STRUCTURE_1u22\| PDB=1u22 \| SCENE= }}		{{STRUCTURE_1u22\| PDB=1u22 \| SCENE= }}
-
	===A. thaliana cobalamine independent methionine synthase===		===A. thaliana cobalamine independent methionine synthase===
		+	{{ABSTRACT_PUBMED_15326182}}

-	~~{{ABSTRACT_PUBMED_15326182}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/METE_ARATH METE_ARATH]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

	==About this Structure==		==About this Structure==
Line 11:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:015326182</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015326182</ref><references group="xtra"/><references/>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]

OCA: Protected "1u22" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 13:27:36 GMT

Protected "1u22" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:27, 5 January 2013

OCA at 13:27, 5 January 2013

OCA — Sat, 05 Jan 2013 13:27:34 GMT

←Older revision		Revision as of 13:27, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1u22.png\|left\|200px]]		[[Image:1u22.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1u22", 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_1u22\| PDB=1u22 \| SCENE= }}		{{STRUCTURE_1u22\| PDB=1u22 \| SCENE= }}

	===A. thaliana cobalamine independent methionine synthase===		===A. thaliana cobalamine independent methionine synthase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15326182}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15326182 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15326182}}		{{ABSTRACT_PUBMED_15326182}}

	==About this Structure==		==About this Structure==
-	~~1U22~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA].	+	[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15326182~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015326182</ref><references group="xtra"/>
	[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]		[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
Line 30:		Line 18:
	[[Category: Ravanel, S.]]		[[Category: Ravanel, S.]]
	[[Category: Robert, M.]]		[[Category: Robert, M.]]
-	[[Category: Methionine~~,synthase,homocysteine,methyltetrahydrofolate~~]]	+	[[Category: Homocysteine]]
-		+	[[Category: Methionine]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 19~~:~~07:52 2009''~~	+	[[Category: Methyltetrahydrofolate]]
		+	[[Category: Synthase]]
		+	[[Category: Transferase]]