3wco - Revision history

OCA at 13:04, 8 November 2023

2023-11-08T13:04:23Z

←Older revision		Revision as of 13:04, 8 November 2023
Line 3:		Line 3:
	<StructureSection load='3wco' size='340' side='right'caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3wco' size='340' side='right'caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Aquae Aquae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WCO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=THJ:THIOSULFATE'>THJ</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]] 2.4Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</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;'>[[3w1h\|3w1h]]~~, ~~[[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]~~<~~/div></td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">aq_1031, selA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [https://pdbe.org/3wco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [https://www.ebi.ac.uk/pdbsum/3wco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wco 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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [https://pdbe.org/3wco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [https://www.ebi.ac.uk/pdbsum/3wco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).	+	[https://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aquae~~]]	+	[[Category: Aquifex aeolicus VF5]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Itoh, Y]]	+	[[Category: Itoh Y]]
-	[[Category: Sekine, S]]	+	[[Category: Sekine S]]
-	[[Category: Yokoyama, S]]	+	[[Category: Yokoyama S]]
-	~~[[Category: Homodimer]]~~	+
-	~~[[Category: Selenium metabolism]]~~	+
-	~~[[Category: Selenocysteine synthesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:31, 3 August 2022

2022-08-03T05:31:41Z

←Older revision		Revision as of 05:31, 3 August 2022
Line 1:		Line 1:

	==Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA==		==Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA==
-	<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='3wco' size='340' side='right'caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3WCO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WCO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [~~http~~://pdbe.org/3wco PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3wco PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3wco 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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [https://pdbe.org/3wco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [https://www.ebi.ac.uk/pdbsum/3wco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).	+	[[https://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Aquae]]		[[Category: Aquae]]
		+	[[Category: Large Structures]]
	[[Category: Itoh, Y]]		[[Category: Itoh, Y]]
	[[Category: Sekine, S]]		[[Category: Sekine, S]]

OCA at 00:47, 5 August 2016

2016-08-05T00:47:11Z

←Older revision		Revision as of 00:47, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA==		==Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA==
	<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
-	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-~~LYSINE(~~3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-~~YLMETHANE)~~'>LLP</scene>, <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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco 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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://pdbe.org/3wco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	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 3wco" style="background-color:#fffaf0;"></div>

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

OCA at 14:28, 25 December 2014

2014-12-25T14:28:48Z

←Older revision		Revision as of 14:28, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>	+	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCO FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <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=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco 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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 18:
	Dimer-Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity.,Itoh Y, Brocker MJ, Sekine SI, Soll D, Yokoyama S J Mol Biol. 2014 Jan 20. pii: S0022-2836(14)00022-9. doi:, 10.1016/j.jmb.2014.01.003. PMID:24456689<ref>PMID:24456689</ref>		Dimer-Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity.,Itoh Y, Brocker MJ, Sekine SI, Soll D, Yokoyama S J Mol Biol. 2014 Jan 20. pii: S0022-2836(14)00022-9. doi:, 10.1016/j.jmb.2014.01.003. PMID:24456689<ref>PMID:24456689</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
		+
		+	==See Also==
		+	*[[Selenocysteine synthase\|Selenocysteine synthase]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Aquae]]		[[Category: Aquae]]
-	[[Category: Itoh, Y.]]	+	[[Category: Itoh, Y]]
-	[[Category: Sekine, S.]]	+	[[Category: Sekine, S]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Homodimer]]		[[Category: Homodimer]]
	[[Category: Selenium metabolism]]		[[Category: Selenium metabolism]]
	[[Category: Selenocysteine synthesis]]		[[Category: Selenocysteine synthesis]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:36, 1 May 2014

2014-05-01T09:36:30Z

←Older revision		Revision as of 09:36, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>	+	<table><tr><td colspan='2'>[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene><br>
-	<b>[[Non-Standard_Residue\|NonStd Res:]]</b> <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><br>	+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<b>[[Related_structure\|Related:]]</b> [[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aq_1031, selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco PDBsum]</span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal 5'-phosphate-dependent enzyme superfamily, has an exceptional homodecameric quaternary structure with a molecular mass of about 500kDa. Our previously determined crystal structures of Aquifex aeolicus SelA complexed with tRNASec revealed that the ring-shaped decamer is composed of pentamerized SelA dimers, with two SelA dimers arranged to collaboratively interact with one Ser-tRNASec. The SelA catalytic site is close to the dimer-dimer interface, but the significance of the dimer pentamerization in the catalytic site formation remained elusive. In the present study, we examined the quaternary interactions and demonstrated their importance for SelA activity by systematic mutagenesis. Furthermore, we determined the crystal structures of "depentamerized" SelA variants with mutations at the dimer-dimer interface that prevent pentamerization. These dimeric SelA variants formed a distorted and inactivated catalytic site and confirmed that the pentamer interactions are essential for productive catalytic site formation. Intriguingly, the conformation of the non-functional active site of dimeric SelA shares structural features with other fold-type-I pyridoxal 5'-phosphate-dependent enzymes with native dimer or tetramer (dimer-of-dimers) quaternary structures.		The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal 5'-phosphate-dependent enzyme superfamily, has an exceptional homodecameric quaternary structure with a molecular mass of about 500kDa. Our previously determined crystal structures of Aquifex aeolicus SelA complexed with tRNASec revealed that the ring-shaped decamer is composed of pentamerized SelA dimers, with two SelA dimers arranged to collaboratively interact with one Ser-tRNASec. The SelA catalytic site is close to the dimer-dimer interface, but the significance of the dimer pentamerization in the catalytic site formation remained elusive. In the present study, we examined the quaternary interactions and demonstrated their importance for SelA activity by systematic mutagenesis. Furthermore, we determined the crystal structures of "depentamerized" SelA variants with mutations at the dimer-dimer interface that prevent pentamerization. These dimeric SelA variants formed a distorted and inactivated catalytic site and confirmed that the pentamer interactions are essential for productive catalytic site formation. Intriguingly, the conformation of the non-functional active site of dimeric SelA shares structural features with other fold-type-I pyridoxal 5'-phosphate-dependent enzymes with native dimer or tetramer (dimer-of-dimers) quaternary structures.
Line 14:		Line 17:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:10, 30 April 2014

2014-04-30T10:10:54Z

←Older revision		Revision as of 10:10, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>		[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>
-	<b>Related:</b> [[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene><br>
		+	<b>[[Non-Standard_Residue\|NonStd Res:]]</b> <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wco RCSB], [http://www.ebi.ac.uk/pdbsum/3wco PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal 5'-phosphate-dependent enzyme superfamily, has an exceptional homodecameric quaternary structure with a molecular mass of about 500kDa. Our previously determined crystal structures of Aquifex aeolicus SelA complexed with tRNASec revealed that the ring-shaped decamer is composed of pentamerized SelA dimers, with two SelA dimers arranged to collaboratively interact with one Ser-tRNASec. The SelA catalytic site is close to the dimer-dimer interface, but the significance of the dimer pentamerization in the catalytic site formation remained elusive. In the present study, we examined the quaternary interactions and demonstrated their importance for SelA activity by systematic mutagenesis. Furthermore, we determined the crystal structures of "depentamerized" SelA variants with mutations at the dimer-dimer interface that prevent pentamerization. These dimeric SelA variants formed a distorted and inactivated catalytic site and confirmed that the pentamer interactions are essential for productive catalytic site formation. Intriguingly, the conformation of the non-functional active site of dimeric SelA shares structural features with other fold-type-I pyridoxal 5'-phosphate-dependent enzymes with native dimer or tetramer (dimer-of-dimers) quaternary structures.		The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal 5'-phosphate-dependent enzyme superfamily, has an exceptional homodecameric quaternary structure with a molecular mass of about 500kDa. Our previously determined crystal structures of Aquifex aeolicus SelA complexed with tRNASec revealed that the ring-shaped decamer is composed of pentamerized SelA dimers, with two SelA dimers arranged to collaboratively interact with one Ser-tRNASec. The SelA catalytic site is close to the dimer-dimer interface, but the significance of the dimer pentamerization in the catalytic site formation remained elusive. In the present study, we examined the quaternary interactions and demonstrated their importance for SelA activity by systematic mutagenesis. Furthermore, we determined the crystal structures of "depentamerized" SelA variants with mutations at the dimer-dimer interface that prevent pentamerization. These dimeric SelA variants formed a distorted and inactivated catalytic site and confirmed that the pentamer interactions are essential for productive catalytic site formation. Intriguingly, the conformation of the non-functional active site of dimeric SelA shares structural features with other fold-type-I pyridoxal 5'-phosphate-dependent enzymes with native dimer or tetramer (dimer-of-dimers) quaternary structures.

OCA at 05:28, 30 April 2014

2014-04-30T05:28:49Z

←Older revision		Revision as of 05:28, 30 April 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3wco\| PDB=3wco \| SCENE= }}~~	+	==Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA==
-	===Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA===	+	<StructureSection load='3wco' size='340' side='right' caption='[[3wco]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	[[3wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA]. <br>
		+	<b>Related:</b> [[3w1h\|3w1h]], [[3w1i\|3w1i]], [[3w1j\|3w1j]], [[3w1k\|3w1k]], [[3wcn\|3wcn]]<br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Publication Abstract from PubMed ==
		+	The 21st amino acid, selenocysteine (Sec), is incorporated translationally into proteins and is synthesized on its specific tRNA (tRNASec). In Bacteria, the selenocysteine synthase SelA converts Ser-tRNASec, formed by seryl-tRNA synthetase, to Sec-tRNASec. SelA, a member of the fold-type-I pyridoxal 5'-phosphate-dependent enzyme superfamily, has an exceptional homodecameric quaternary structure with a molecular mass of about 500kDa. Our previously determined crystal structures of Aquifex aeolicus SelA complexed with tRNASec revealed that the ring-shaped decamer is composed of pentamerized SelA dimers, with two SelA dimers arranged to collaboratively interact with one Ser-tRNASec. The SelA catalytic site is close to the dimer-dimer interface, but the significance of the dimer pentamerization in the catalytic site formation remained elusive. In the present study, we examined the quaternary interactions and demonstrated their importance for SelA activity by systematic mutagenesis. Furthermore, we determined the crystal structures of "depentamerized" SelA variants with mutations at the dimer-dimer interface that prevent pentamerization. These dimeric SelA variants formed a distorted and inactivated catalytic site and confirmed that the pentamer interactions are essential for productive catalytic site formation. Intriguingly, the conformation of the non-functional active site of dimeric SelA shares structural features with other fold-type-I pyridoxal 5'-phosphate-dependent enzymes with native dimer or tetramer (dimer-of-dimers) quaternary structures.

-	~~==Function==~~	+	Dimer-Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity.,Itoh Y, Brocker MJ, Sekine SI, Soll D, Yokoyama S J Mol Biol. 2014 Jan 20. pii: S0022-2836(14)00022-9. doi:, 10.1016/j.jmb.2014.01.003. PMID:24456689<ref>PMID:24456689</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl~~-~~tRNA~~(~~Sec~~) ~~to selenocysteinyl~~-~~tRNA(Sec) required for selenoprotein biosynthesis (By similarity)~~.	+

-	==~~About this Structure~~==	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	[[~~3wco~~]] ~~is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA].~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Aquae]]
	[[Category: Itoh, Y.]]		[[Category: Itoh, Y.]]
	[[Category: Sekine, S.]]		[[Category: Sekine, S.]]

OCA at 07:00, 22 January 2014

2014-01-22T07:00:29Z

←Older revision		Revision as of 07:00, 22 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3wco\| PDB=3wco \| SCENE= }}
		+	===Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA===

-	~~The entry 3wco is ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).

-	~~Authors~~: Itoh, Y., Sekine, S., Yokoyama, S.	+	==About this Structure==
-		+	[[3wco]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCO OCA].
-	~~Description~~: ~~Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA~~	+	[[Category: Itoh, Y.]]
		+	[[Category: Sekine, S.]]
		+	[[Category: Yokoyama, S.]]
		+	[[Category: Homodimer]]
		+	[[Category: Selenium metabolism]]
		+	[[Category: Selenocysteine synthesis]]
		+	[[Category: Transferase]]

OCA: Protected "3wco" [edit=sysop:move=sysop]

2013-06-19T10:40:35Z

Protected "3wco" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:40, 19 June 2013

OCA: New page: '''Unreleased structure''' The entry 3wco is ON HOLD until Paper Publication Authors: Itoh, Y., Sekine, S., Yokoyama, S. Description: Crystal structure of the depentamerized mutant of ...

2013-06-19T10:40:34Z

New page: '''Unreleased structure''' The entry 3wco is ON HOLD until Paper Publication Authors: Itoh, Y., Sekine, S., Yokoyama, S. Description: Crystal structure of the depentamerized mutant of ...

New page

'''Unreleased structure'''

The entry 3wco is ON HOLD until Paper Publication

Authors: Itoh, Y., Sekine, S., Yokoyama, S.

Description: Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA