4k87 - Revision history

OCA at 14:28, 8 November 2023

OCA — Wed, 08 Nov 2023 14:28:48 GMT

←Older revision		Revision as of 14:28, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K87 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K87 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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]] 2.301Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [https://pdbe.org/4k87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [https://www.ebi.ac.uk/pdbsum/4k87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k87 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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [https://pdbe.org/4k87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [https://www.ebi.ac.uk/pdbsum/4k87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k87 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:44, 30 November 2022

OCA — Wed, 30 Nov 2022 11:44:46 GMT

←Older revision		Revision as of 11:44, 30 November 2022
Line 3:		Line 3:
	<StructureSection load='4k87' size='340' side='right'caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4k87' size='340' side='right'caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4K87 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K87 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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">[[4k86\|4k86]], [[4k88\|4k88]]</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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [https://pdbe.org/4k87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [https://www.ebi.ac.uk/pdbsum/4k87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k87 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [~~http~~://pdbe.org/4k87 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4k87 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4k87 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN]] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>	+	[https://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Proline--tRNA ligase]]~~	+	[[Category: Hwang KY]]
-	[[Category: Hwang~~, K Y~~]]	+	[[Category: Lee EH]]
-	[[Category: Lee~~, E H~~]]	+	[[Category: Son JH]]
-	[[Category: Son~~, J H]]~~	+
-	~~[[Category: Class ii trna synthetase]]~~	+
-	~~[[Category: Cytosol]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Zinc binding~~]]	+

OCA at 10:03, 25 December 2019

OCA — Wed, 25 Dec 2019 10:03:26 GMT

←Older revision		Revision as of 10:03, 25 December 2019
Line 1:		Line 1:

	==Crystal structure of human prolyl-tRNA synthetase (substrate bound form)==		==Crystal structure of human prolyl-tRNA synthetase (substrate bound form)==
-	<StructureSection load='4k87' size='340' side='right' caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4k87' size='340' side='right'caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K87 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K87 FirstGlance]. <br>
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN]] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>		[[http://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN]] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Aminoacyl-tRNA synthetases recognize cognate amino acids and tRNAs from their noncognate counterparts and catalyze the formation of aminoacyl-tRNAs. Halofuginone (HF), a coccidiostat used in veterinary medicine, exerts its effects by acting as a high-affinity inhibitor of the enzyme glutamyl-prolyl-tRNA synthetase (EPRS). In order to elucidate the precise molecular basis of this inhibition mechanism of human EPRS, the crystal structures of the prolyl-tRNA synthetase domain of human EPRS (hPRS) at 2.4 A resolution (hPRS-apo), of hPRS complexed with ATP and the substrate proline at 2.3 A resolution (hPRS-sub) and of hPRS complexed with HF at 2.62 A resolution (hPRS-HF) are presented. These structures show plainly that motif 1 functions as a cap in hPRS, which is loosely opened in hPRS-apo, tightly closed in hPRS-sub and incorrectly closed in hPRS-HF. In addition, the structural analyses are consistent with more effective binding of hPRS to HF with ATP. Mutagenesis and biochemical analysis confirmed the key roles of two residues, Phe1097 and Arg1152, in the HF inhibition mechanism. These structures will lead to the development of more potent and selective hPRS inhibitors for promoting inflammatory resolution.
		+
		+	Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone.,Son J, Lee EH, Park M, Kim JH, Kim J, Kim S, Jeon YH, Hwang KY Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2136-45. doi:, 10.1107/S0907444913020556. Epub 2013 Sep 20. PMID:24100331<ref>PMID:24100331</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4k87" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminoacyl tRNA synthetase 3D structures\|Aminoacyl tRNA synthetase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 17:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Proline--tRNA ligase]]		[[Category: Proline--tRNA ligase]]
	[[Category: Hwang, K Y]]		[[Category: Hwang, K Y]]

OCA at 19:36, 5 August 2016

OCA — Fri, 05 Aug 2016 19:36:12 GMT

←Older revision		Revision as of 19:36, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human prolyl-tRNA synthetase (substrate bound form)==		==Crystal structure of human prolyl-tRNA synthetase (substrate bound form)==
	<StructureSection load='4k87' size='340' side='right' caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4k87' size='340' side='right' caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K87 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K87 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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">[[4k86\|4k86]], [[4k88\|4k88]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4k86\|4k86]], [[4k88\|4k88]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [http://www.ebi.ac.uk/pdbsum/4k87 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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [http://pdbe.org/4k87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [http://www.ebi.ac.uk/pdbsum/4k87 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k87 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Proline--tRNA ligase]]		[[Category: Proline--tRNA ligase]]
	[[Category: Hwang, K Y]]		[[Category: Hwang, K Y]]

OCA at 21:21, 25 December 2014

OCA — Thu, 25 Dec 2014 21:21:11 GMT

←Older revision		Revision as of 21:21, 25 December 2014
Line 9:		Line 9:
	<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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [http://www.ebi.ac.uk/pdbsum/4k87 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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [http://www.ebi.ac.uk/pdbsum/4k87 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN]] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:07, 21 December 2014

OCA — Sun, 21 Dec 2014 15:07:32 GMT

←Older revision		Revision as of 15:07, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4k87\| PDB=4k87 \| SCENE= }}~~	+	==Crystal structure of human prolyl-tRNA synthetase (substrate bound form)==
-	===Crystal structure of human prolyl-tRNA synthetase (substrate bound form)===	+	<StructureSection load='4k87' size='340' side='right' caption='[[4k87]], [[Resolution\|resolution]] 2.30Å' scene=''>
-		+	== Structural highlights ==
-	==~~Function~~==	+	<table><tr><td colspan='2'>[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K87 FirstGlance]. <br>
-	[[http://~~www~~.~~uniprot~~.org/~~uniprot~~/~~SYEP_HUMAN SYEP_HUMAN~~]] ~~Catalyzes the attachment of~~ the ~~cognate amino acid to the corresponding tRNA in a two-step reaction~~: ~~the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA~~. ~~Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes~~. ~~Upon interferon~~-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<~~ref~~>~~PMID~~:~~1756734~~</~~ref~~> <~~ref~~>~~PMID~~:~~15479637~~</~~ref~~> <~~ref~~>~~PMID~~:~~23071094~~</~~ref~~>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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">[[4k86\|4k86]], [[4k88\|4k88]]</td></tr>
-	==~~About this Structure=~~=	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	[[~~4k87~~]] ~~is a 1 chain structure with sequence from~~ [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. ~~Full crystallographic information is available from~~ [http://oca.weizmann.ac.il/oca-bin/~~ocashort~~?id=~~4K87~~ OCA].	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </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=4k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k87 RCSB], [http://www.ebi.ac.uk/pdbsum/4k87 PDBsum]</span></td></tr>
-	~~==Reference=~~=	+	</table>
-	<~~references group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Proline--tRNA ligase]]		[[Category: Proline--tRNA ligase]]
-	[[Category: Hwang, K Y.]]	+	[[Category: Hwang, K Y]]
-	[[Category: Lee, E H.]]	+	[[Category: Lee, E H]]
-	[[Category: Son, J H.]]	+	[[Category: Son, J H]]
	[[Category: Class ii trna synthetase]]		[[Category: Class ii trna synthetase]]
	[[Category: Cytosol]]		[[Category: Cytosol]]
	[[Category: Ligase]]		[[Category: Ligase]]
	[[Category: Zinc binding]]		[[Category: Zinc binding]]

OCA at 06:39, 10 October 2013

OCA — Thu, 10 Oct 2013 06:39:33 GMT

←Older revision		Revision as of 06:39, 10 October 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4k87\| PDB=4k87 \| SCENE= }}
		+	===Crystal structure of human prolyl-tRNA synthetase (substrate bound form)===

-	~~The entry 4k87~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/SYEP_HUMAN SYEP_HUMAN]] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:1756734</ref> <ref>PMID:15479637</ref> <ref>PMID:23071094</ref>

-	~~Authors~~: ~~Hwang, K~~.Y.~~, Son, J~~.H.~~, Lee, E~~.H.	+	==About this Structure==
		+	[[4k87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K87 OCA].

-	~~Description~~: ~~Crystal structure of human prolyl~~-tRNA synthetase ~~(substrate bound form)~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Proline--tRNA ligase]]
		+	[[Category: Hwang, K Y.]]
		+	[[Category: Lee, E H.]]
		+	[[Category: Son, J H.]]
		+	[[Category: Class ii trna synthetase]]
		+	[[Category: Cytosol]]
		+	[[Category: Ligase]]
		+	[[Category: Zinc binding]]

OCA at 11:29, 19 June 2013

OCA — Wed, 19 Jun 2013 11:29:29 GMT

←Older revision		Revision as of 11:29, 19 June 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4k87 is ON HOLD	+	The entry 4k87 is ON HOLD until Paper Publication

	Authors: Hwang, K.Y., Son, J.H., Lee, E.H.		Authors: Hwang, K.Y., Son, J.H., Lee, E.H.

	Description: Crystal structure of human prolyl-tRNA synthetase (substrate bound form)		Description: Crystal structure of human prolyl-tRNA synthetase (substrate bound form)

OCA at 06:53, 16 May 2013

OCA — Thu, 16 May 2013 06:53:43 GMT

←Older revision		Revision as of 06:53, 16 May 2013
Line 3:		Line 3:
	The entry 4k87 is ON HOLD		The entry 4k87 is ON HOLD

-	Authors: Hwang, K.Y., Son, JH, Lee, E.H.	+	Authors: Hwang, K.Y., Son, J.H., Lee, E.H.

	Description: Crystal structure of human prolyl-tRNA synthetase (substrate bound form)		Description: Crystal structure of human prolyl-tRNA synthetase (substrate bound form)

OCA: Protected "4k87" [edit=sysop:move=sysop]

OCA — Wed, 24 Apr 2013 11:02:39 GMT

Protected "4k87" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:02, 24 April 2013