5tdz - Revision history

OCA at 15:40, 6 March 2024

OCA — Wed, 06 Mar 2024 15:40:31 GMT

←Older revision		Revision as of 15:40, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='5tdz' size='340' side='right'caption='[[5tdz]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5tdz' size='340' side='right'caption='[[5tdz]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tdz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5TDZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tdz]] is a 2 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=5TDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDZ 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5te1\|5te1]]</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=5tdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdz OCA], [https://pdbe.org/5tdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdz RCSB], [https://www.ebi.ac.uk/pdbsum/5tdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdz 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/ATP_citrate_synthase ATP citrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.8 2.3.3.8] </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=5tdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdz OCA], [~~http~~://pdbe.org/5tdz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tdz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tdz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ACLY_HUMAN ACLY_HUMAN]] ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.<ref>PMID:23932781</ref>	+	[https://www.uniprot.org/uniprot/ACLY_HUMAN ACLY_HUMAN] ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.<ref>PMID:23932781</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Hydroxycitrate from the fruit of Garcinia cambogia [i.e. (2S,3S)-2-hydroxycitrate] is the best-known inhibitor of ATP-citrate lyase. Well diffracting crystals showing how the inhibitor binds to human ATP-citrate lyase were grown by modifying the protein. The protein was modified by introducing cleavage sites for Tobacco etch virus protease on either side of a disordered linker. The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen. For the first time, electron density was evident for the loop that contains His760, which is phosphorylated as part of the catalytic mechanism. The pro-S carboxylate of (2S,3S)-2-hydroxycitrate is available to accept a phosphoryl group from His760. However, when co-crystals were grown with ATP and magnesium ions as well as either the inhibitor or citrate, Mg2+-ADP was bound and His760 was phosphorylated. The phosphoryl group was not transferred to the organic acid. This led to the interpretation that the active site is trapped in an open conformation. The strategy of designing cleavage sites to remove disordered residues could be useful in determining the crystal structures of other proteins.	+
-		+
-	Binding of hydroxycitrate to human ATP-citrate lyase.,Hu J, Komakula A, Fraser ME Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):660-671. doi:, 10.1107/S2059798317009871. Epub 2017 Jul 28. PMID:28777081<ref>PMID:28777081</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5tdz" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~ATP citrate synthase~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fraser~~, M E~~]]	+	[[Category: Fraser ME]]
-	[[Category: Hu, J]]	+	[[Category: Hu J]]
-	~~[[Category: Atp-grasp fold]]~~	+
-	~~[[Category: Tartrate binding]]~~	+
-	~~[[Category: Tev cleaved]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:30, 16 September 2020

OCA — Wed, 16 Sep 2020 11:30:44 GMT

←Older revision		Revision as of 11:30, 16 September 2020
Line 1:		Line 1:

	==TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP==		==TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP==
-	<StructureSection load='5tdz' size='340' side='right' caption='[[5tdz]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5tdz' size='340' side='right'caption='[[5tdz]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tdz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDZ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TDZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tdz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TDZ 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5te1\|5te1]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5te1\|5te1]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_citrate_synthase ATP citrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.8 2.3.3.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_citrate_synthase ATP citrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.8 2.3.3.8] </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=5tdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdz OCA], [http://pdbe.org/5tdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdz RCSB], [http://www.ebi.ac.uk/pdbsum/5tdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdz 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=5tdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdz OCA], [http://pdbe.org/5tdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdz RCSB], [http://www.ebi.ac.uk/pdbsum/5tdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5tdz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tdz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATP-citrate synthase 3D structures\|ATP-citrate synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: ATP citrate synthase]]		[[Category: ATP citrate synthase]]
		+	[[Category: Large Structures]]
	[[Category: Fraser, M E]]		[[Category: Fraser, M E]]
	[[Category: Hu, J]]		[[Category: Hu, J]]

OCA at 05:56, 17 August 2017

OCA — Thu, 17 Aug 2017 05:56:14 GMT

←Older revision		Revision as of 05:56, 17 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5tdz is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP==
		+	<StructureSection load='5tdz' size='340' side='right' caption='[[5tdz]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5tdz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDZ 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5te1\|5te1]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_citrate_synthase ATP citrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.8 2.3.3.8] </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=5tdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdz OCA], [http://pdbe.org/5tdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdz RCSB], [http://www.ebi.ac.uk/pdbsum/5tdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdz ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACLY_HUMAN ACLY_HUMAN]] ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.<ref>PMID:23932781</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Hydroxycitrate from the fruit of Garcinia cambogia [i.e. (2S,3S)-2-hydroxycitrate] is the best-known inhibitor of ATP-citrate lyase. Well diffracting crystals showing how the inhibitor binds to human ATP-citrate lyase were grown by modifying the protein. The protein was modified by introducing cleavage sites for Tobacco etch virus protease on either side of a disordered linker. The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen. For the first time, electron density was evident for the loop that contains His760, which is phosphorylated as part of the catalytic mechanism. The pro-S carboxylate of (2S,3S)-2-hydroxycitrate is available to accept a phosphoryl group from His760. However, when co-crystals were grown with ATP and magnesium ions as well as either the inhibitor or citrate, Mg2+-ADP was bound and His760 was phosphorylated. The phosphoryl group was not transferred to the organic acid. This led to the interpretation that the active site is trapped in an open conformation. The strategy of designing cleavage sites to remove disordered residues could be useful in determining the crystal structures of other proteins.

-	~~Authors: Hu~~, J., Fraser, M.E.	+	Binding of hydroxycitrate to human ATP-citrate lyase.,Hu J, Komakula A, Fraser ME Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):660-671. doi:, 10.1107/S2059798317009871. Epub 2017 Jul 28. PMID:28777081<ref>PMID:28777081</ref>

-	~~Description~~: ~~TEV Cleaved Human~~ ATP ~~Citrate Lyase Bound to Tartrate and ADP~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5tdz" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: ATP citrate synthase]]
		+	[[Category: Fraser, M E]]
	[[Category: Hu, J]]		[[Category: Hu, J]]
-	[[Category: ~~Fraser, M.E~~]]	+	[[Category: Atp-grasp fold]]
		+	[[Category: Tartrate binding]]
		+	[[Category: Tev cleaved]]
		+	[[Category: Transferase]]

OCA at 13:29, 9 March 2017

OCA — Thu, 09 Mar 2017 13:29:56 GMT

←Older revision		Revision as of 13:29, 9 March 2017
Line 7:		Line 7:
	Description: TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP		Description: TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Fraser, M.E]]
	[[Category: Hu, J]]		[[Category: Hu, J]]
		+	[[Category: Fraser, M.E]]

OCA at 16:58, 26 October 2016

OCA — Wed, 26 Oct 2016 16:58:11 GMT

←Older revision		Revision as of 16:58, 26 October 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Hu, J., Fraser, M.E.		Authors: Hu, J., Fraser, M.E.

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

OCA — Mon, 03 Oct 2016 15:31:50 GMT

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

←Older revision

Revision as of 15:31, 3 October 2016

OCA: New page: '''Unreleased structure''' The entry 5tdz is ON HOLD Authors: Hu, J., Fraser, M.E. Description: TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP [[Category: Unreleased Str...

OCA — Mon, 03 Oct 2016 15:31:49 GMT

New page: '''Unreleased structure''' The entry 5tdz is ON HOLD Authors: Hu, J., Fraser, M.E. Description: TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP [[Category: Unreleased Str...

New page

'''Unreleased structure'''

The entry 5tdz is ON HOLD

Authors: Hu, J., Fraser, M.E.

Description: TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP
[[Category: Unreleased Structures]]
[[Category: Fraser, M.E]]
[[Category: Hu, J]]