5t5s - Revision history

OCA at 12:54, 4 October 2023

OCA — Wed, 04 Oct 2023 12:54:55 GMT

←Older revision		Revision as of 12:54, 4 October 2023
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	<StructureSection load='5t5s' size='340' side='right'caption='[[5t5s]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5t5s' size='340' side='right'caption='[[5t5s]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5t5s]] 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=5T5S OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5T5S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5t5s]] 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=5T5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T5S FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>AARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=9606 HUMAN])</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]] 2.202Å</td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine~~-~~-tRNA_ligase Alanine--tRNA ligase]~~, ~~with EC number~~ [~~http://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </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=5t5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5s OCA], [https://pdbe.org/5t5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t5s RCSB], [https://www.ebi.ac.uk/pdbsum/5t5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5s 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=5t5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5s OCA], [~~http~~://pdbe.org/5t5s PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5t5s RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5t5s PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5s ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]	+	[https://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
	<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: ~~Alanine--tRNA ligase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Schimmel, P]]	+	[[Category: Schimmel P]]
-	[[Category: Sun, L]]	+	[[Category: Sun L]]
-	~~[[Category: Translation]]~~	+
-	~~[[Category: Trna synthetase~~]]	+

OCA at 11:22, 16 September 2020

OCA — Wed, 16 Sep 2020 11:22:56 GMT

←Older revision		Revision as of 11:22, 16 September 2020
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	==A fragment of a human tRNA synthetase==		==A fragment of a human tRNA synthetase==
-	<StructureSection load='5t5s' size='340' side='right' caption='[[5t5s]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5t5s' size='340' side='right'caption='[[5t5s]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5t5s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5S OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5T5S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5t5s]] 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=5T5S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T5S FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5t5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5s OCA], [http://pdbe.org/5t5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5s RCSB], [http://www.ebi.ac.uk/pdbsum/5t5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5s ProSAT]</span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </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=5t5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5s OCA], [http://pdbe.org/5t5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5s RCSB], [http://www.ebi.ac.uk/pdbsum/5t5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5s ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</div>		</div>
	<div class="pdbe-citations 5t5s" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5t5s" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminoacyl tRNA synthetase 3D structures\|Aminoacyl tRNA synthetase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Alanine--tRNA ligase]]		[[Category: Alanine--tRNA ligase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Schimmel, P]]		[[Category: Schimmel, P]]
	[[Category: Sun, L]]		[[Category: Sun, L]]
	[[Category: Translation]]		[[Category: Translation]]
	[[Category: Trna synthetase]]		[[Category: Trna synthetase]]

OCA at 09:35, 4 January 2017

OCA — Wed, 04 Jan 2017 09:35:59 GMT

←Older revision		Revision as of 09:35, 4 January 2017
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]		[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 20 aminoacyl tRNA synthetases (aaRSs) couple each amino acid to their cognate tRNAs. During evolution, 19 aaRSs expanded by acquiring novel noncatalytic appended domains, which are absent from bacteria and many lower eukaryotes but confer extracellular and nuclear functions in higher organisms. AlaRS is the single exception, with an appended C-terminal domain (C-Ala) that is conserved from prokaryotes to humans but with a wide sequence divergence. In human cells, C-Ala is also a splice variant of AlaRS. Crystal structures of two forms of human C-Ala, and small-angle X-ray scattering of AlaRS, showed that the large sequence divergence of human C-Ala reshaped C-Ala in a way that changed the global architecture of AlaRS. This reshaping removes the role of C-Ala in prokaryotes for docking tRNA and instead repurposes it to form a dimer interface presenting a DNA-binding groove. This groove cannot form with the bacterial ortholog. Direct DNA binding by human C-Ala, but not by bacterial C-Ala, was demonstrated. Thus, instead of acquiring a novel appended domain like other human aaRSs, which engendered novel functions, a new AlaRS architecture was created by diversifying a preexisting appended domain.
		+
		+	Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS.,Sun L, Song Y, Blocquel D, Yang XL, Schimmel P Proc Natl Acad Sci U S A. 2016 Dec 13;113(50):14300-14305. Epub 2016 Nov 28. PMID:27911835<ref>PMID:27911835</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5t5s" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:38, 10 December 2016

OCA — Sat, 10 Dec 2016 18:38:47 GMT

←Older revision		Revision as of 18:38, 10 December 2016
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-	'''Unreleased structure'''

-	~~The entry~~ 5t5s is ~~ON HOLD~~ ~~until Paper Publication~~	+	==A fragment of a human tRNA synthetase==
-		+	<StructureSection load='5t5s' size='340' side='right' caption='[[5t5s]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5t5s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T5S FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=5t5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5s OCA], [http://pdbe.org/5t5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5s RCSB], [http://www.ebi.ac.uk/pdbsum/5t5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5s ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Alanine--tRNA ligase]]
		+	[[Category: Schimmel, P]]
		+	[[Category: Sun, L]]
		+	[[Category: Translation]]
		+	[[Category: Trna synthetase]]

OCA at 12:14, 21 September 2016

OCA — Wed, 21 Sep 2016 12:14:50 GMT

←Older revision		Revision as of 12:14, 21 September 2016
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5t5s is ON HOLD	+	The entry 5t5s is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5t5s" [edit=sysop:move=sysop]

OCA — Fri, 09 Sep 2016 15:45:10 GMT

Protected "5t5s" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:45, 9 September 2016

OCA: New page: '''Unreleased structure''' The entry 5t5s is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Sep 2016 15:45:08 GMT

New page: '''Unreleased structure''' The entry 5t5s is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5t5s is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]