3qww - Revision history

OCA at 10:50, 21 February 2024

OCA — Wed, 21 Feb 2024 10:50:32 GMT

←Older revision		Revision as of 10:50, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3qww' size='340' side='right'caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3qww' size='340' side='right'caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWW FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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]] 1.8Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Smyd2 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=10090 LK3 transgenic mice])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [https://pdbe.org/3qww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [https://www.ebi.ac.uk/pdbsum/3qww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww 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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [https://pdbe.org/3qww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [https://www.ebi.ac.uk/pdbsum/3qww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref>	+	[https://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	SmyD2 belongs to a new class of chromatin regulators that control gene expression in heart development and tumorigenesis. Besides methylation of histone H3 K4, SmyD2 can methylate non-histone targets including p53 and the retinoblastoma tumor suppressor. The methyltransferase activity of SmyD proteins has been proposed to be regulated by autoinhibition via the intra- and interdomain bending of the conserved C-terminal domain (CTD). However, there has been no direct evidence of a conformational change in the CTD. Here, we report two crystal structures of SmyD2 bound either to the cofactor product S-adenosylhomocysteine or to the inhibitor sinefungin. SmyD2 has a two-lobed structure with the active site located at the bottom of a deep crevice formed between the CTD and the catalytic domain. By extensive engagement with the methyltransferase domain, the CTD stabilizes the autoinhibited conformation of SmyD2 and restricts access to the catalytic site. Unexpectedly, despite that the two SmyD2 structures are highly superimposable, significant differences are observed in the first two helices of the CTDs: the two helices bend outwards and move away from the catalytic domain to generate a less closed conformation in the sinefungin-bound structure. Although the overall fold of the individual domains is structurally conserved among SmyD proteins, SmyD2 appear to be a conformational "intermediate" between a close form of SmyD3 and an open form of SmyD1. In addition, the structures reveal that the CTD is structurally similar to tetratricopeptide repeats (TPR), a motif through which many cochaperones bind to the heat shock protein Hsp90. Our results thus provide the first evidence for the intradomain flexibility of the TPR-like CTD, which may be important for the activation of SmyD proteins by Hsp90.	+
-		+
-	Crystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain.,Jiang Y, Sirinupong N, Brunzelle J, Yang Z PLoS One. 2011;6(6):e21640. Epub 2011 Jun 28. PMID:21738746<ref>PMID:21738746</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3qww" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 15:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Brunzelle, J]]	+	[[Category: Brunzelle J]]
-	[[Category: Jiang, Y]]	+	[[Category: Jiang Y]]
-	[[Category: Sirinupong, N]]	+	[[Category: Sirinupong N]]
-	[[Category: Yang, Z]]	+	[[Category: Yang Z]]
-	~~[[Category: Hsp90]]~~	+
-	~~[[Category: Methyltransferase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 05:39, 15 June 2022

OCA — Wed, 15 Jun 2022 05:39:50 GMT

←Older revision		Revision as of 05:39, 15 June 2022
Line 1:		Line 1:

	==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin==		==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin==
-	<StructureSection load='3qww' size='340' side='right' caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3qww' size='340' side='right'caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3QWW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [~~http~~://pdbe.org/3qww PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3qww PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww 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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [https://pdbe.org/3qww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [https://www.ebi.ac.uk/pdbsum/3qww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref>	+	[[https://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Brunzelle, J]]		[[Category: Brunzelle, J]]

OCA at 02:43, 5 August 2016

OCA — Fri, 05 Aug 2016 02:43:10 GMT

←Older revision		Revision as of 02:43, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin==		==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin==
	<StructureSection load='3qww' size='340' side='right' caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3qww' size='340' side='right' caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [http://www.ebi.ac.uk/pdbsum/3qww 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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [http://pdbe.org/3qww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [http://www.ebi.ac.uk/pdbsum/3qww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 3qww" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Brunzelle, J]]		[[Category: Brunzelle, J]]
	[[Category: Jiang, Y]]		[[Category: Jiang, Y]]

OCA at 22:07, 24 December 2014

OCA — Wed, 24 Dec 2014 22:07:49 GMT

←Older revision		Revision as of 22:07, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWW FirstGlance]. <br>		<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWW FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [http://www.ebi.ac.uk/pdbsum/3qww 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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [http://www.ebi.ac.uk/pdbsum/3qww PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	Crystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain.,Jiang Y, Sirinupong N, Brunzelle J, Yang Z PLoS One. 2011;6(6):e21640. Epub 2011 Jun 28. PMID:21738746<ref>PMID:21738746</ref>		Crystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain.,Jiang Y, Sirinupong N, Brunzelle J, Yang Z PLoS One. 2011;6(6):e21640. Epub 2011 Jun 28. PMID:21738746<ref>PMID:21738746</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>
	== References ==		== References ==
Line 20:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Brunzelle, J.]]	+	[[Category: Brunzelle, J]]
-	[[Category: Jiang, Y.]]	+	[[Category: Jiang, Y]]
-	[[Category: Sirinupong, N.]]	+	[[Category: Sirinupong, N]]
-	[[Category: Yang, Z.]]	+	[[Category: Yang, Z]]
	[[Category: Hsp90]]		[[Category: Hsp90]]
	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 04:44, 5 June 2014

OCA — Thu, 05 Jun 2014 04:44:06 GMT

←Older revision		Revision as of 04:44, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3qww.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin==
		+	<StructureSection load='3qww' size='340' side='right' caption='[[3qww]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QWW FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Smyd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [http://www.ebi.ac.uk/pdbsum/3qww PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SmyD2 belongs to a new class of chromatin regulators that control gene expression in heart development and tumorigenesis. Besides methylation of histone H3 K4, SmyD2 can methylate non-histone targets including p53 and the retinoblastoma tumor suppressor. The methyltransferase activity of SmyD proteins has been proposed to be regulated by autoinhibition via the intra- and interdomain bending of the conserved C-terminal domain (CTD). However, there has been no direct evidence of a conformational change in the CTD. Here, we report two crystal structures of SmyD2 bound either to the cofactor product S-adenosylhomocysteine or to the inhibitor sinefungin. SmyD2 has a two-lobed structure with the active site located at the bottom of a deep crevice formed between the CTD and the catalytic domain. By extensive engagement with the methyltransferase domain, the CTD stabilizes the autoinhibited conformation of SmyD2 and restricts access to the catalytic site. Unexpectedly, despite that the two SmyD2 structures are highly superimposable, significant differences are observed in the first two helices of the CTDs: the two helices bend outwards and move away from the catalytic domain to generate a less closed conformation in the sinefungin-bound structure. Although the overall fold of the individual domains is structurally conserved among SmyD proteins, SmyD2 appear to be a conformational "intermediate" between a close form of SmyD3 and an open form of SmyD1. In addition, the structures reveal that the CTD is structurally similar to tetratricopeptide repeats (TPR), a motif through which many cochaperones bind to the heat shock protein Hsp90. Our results thus provide the first evidence for the intradomain flexibility of the TPR-like CTD, which may be important for the activation of SmyD proteins by Hsp90.

-	<!--	+	Crystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain.,Jiang Y, Sirinupong N, Brunzelle J, Yang Z PLoS One. 2011;6(6):e21640. Epub 2011 Jun 28. PMID:21738746<ref>PMID:21738746</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3qww"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_3qww\| PDB=3qww \| SCENE= }}~~	+

-	~~===Crystal structure~~ of ~~histone lysine methyltransferase SmyD2 in complex with~~ the ~~methyltransferase inhibitor sinefungin===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21738746}}, adds the Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21738746 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_21738746}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3qww]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021738746<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Brunzelle, J.]]		[[Category: Brunzelle, J.]]

OCA at 06:22, 21 March 2012

OCA — Wed, 21 Mar 2012 06:22:30 GMT

←Older revision		Revision as of 06:22, 21 March 2012
Line 1:		Line 1:
-	[[Image:3qww.~~jpg~~\|left\|200px]]	+	[[Image:3qww.png\|left\|200px]]

	<!--		<!--
Line 11:		Line 11:
	===Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin===		===Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21738746}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21738746 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21738746}}

	==About this Structure==		==About this Structure==
	[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA].		[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021738746</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Brunzelle, J.]]		[[Category: Brunzelle, J.]]

OCA at 19:00, 6 July 2011

OCA — Wed, 06 Jul 2011 19:00:41 GMT

←Older revision		Revision as of 19:00, 6 July 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3qww.jpg\|left\|200px]]

-	The ~~entry 3qww~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3qww", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3qww\| PDB=3qww \| SCENE= }}

-	~~Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z.~~	+	===Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin===

-	~~Description: Crystal~~ structure ~~of histone lysine methyltransferase SmyD2 in complex~~ with ~~the methyltransferase~~ inhibitor ~~sinefungin~~	+
		+	==About this Structure==
		+	[[3qww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA].
		+	[[Category: Mus musculus]]
		+	[[Category: Brunzelle, J.]]
		+	[[Category: Jiang, Y.]]
		+	[[Category: Sirinupong, N.]]
		+	[[Category: Yang, Z.]]
		+	[[Category: Hsp90]]
		+	[[Category: Methyltransferase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 08:04, 16 March 2011

OCA — Wed, 16 Mar 2011 08:04:44 GMT

←Older revision		Revision as of 08:04, 16 March 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qww is ON HOLD	+	The entry 3qww is ON HOLD until Paper Publication

	Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z.		Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z.

	Description: Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin		Description: Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin

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

OCA — Wed, 09 Mar 2011 06:09:29 GMT

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

←Older revision

Revision as of 06:09, 9 March 2011

OCA: New page: '''Unreleased structure''' The entry 3qww is ON HOLD Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z. Description: Crystal structure of histone lysine methyltransferase SmyD...

OCA — Wed, 09 Mar 2011 06:09:28 GMT

New page: '''Unreleased structure''' The entry 3qww is ON HOLD Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z. Description: Crystal structure of histone lysine methyltransferase SmyD...

New page

'''Unreleased structure'''

The entry 3qww is ON HOLD

Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z.

Description: Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin