1peg: Difference between revisions

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-{{Seed}}
-[[Image:1peg.png|left|200px]]
-<!--
+==Structural basis for the product specificity of histone lysine methyltransferases==
-The line below this paragraph, containing "STRUCTURE_1peg", creates the "Structure Box" on the page.
+<StructureSection load='1peg' size='340' side='right'caption='[[1peg]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1peg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1peg|  PDB=1peg  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peg OCA], [https://pdbe.org/1peg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1peg RCSB], [https://www.ebi.ac.uk/pdbsum/1peg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1peg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DIM5_NEUCR DIM5_NEUCR] Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.<ref>PMID:11713521</ref> <ref>PMID:12679815</ref> <ref>PMID:12372305</ref> <ref>PMID:12887903</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1peg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1peg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+DIM-5 is a SUV39-type histone H3 Lys9 methyltransferase that is essential for DNA methylation in N. crassa. We report the structure of a ternary complex including DIM-5, S-adenosyl-L-homocysteine, and a substrate H3 peptide. The histone tail inserts as a parallel strand between two DIM-5 strands, completing a hybrid sheet. Three post-SET cysteines coordinate a zinc atom together with Cys242 from the SET signature motif (NHXCXPN) near the active site. Consequently, a narrow channel is formed to accommodate the target Lys9 side chain. The sulfur atom of S-adenosyl-L-homocysteine, where the transferable methyl group is to be attached in S-adenosyl-L-methionine, lies at the opposite end of the channel, approximately 4 A away from the target Lys9 nitrogen. Structural comparison of the active sites of DIM-5, an H3 Lys9 trimethyltransferase, and SET7/9, an H3 Lys4 monomethyltransferase, allowed us to design substitutions in both enzymes that profoundly alter their product specificities without affecting their catalytic activities.
-===Structural basis for the product specificity of histone lysine methyltransferases===
+Structural basis for the product specificity of histone lysine methyltransferases.,Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X Mol Cell. 2003 Jul;12(1):177-85. PMID:12887903<ref>PMID:12887903</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1peg" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_12887903}}, adds the Publication Abstract to the page
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 12887903 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12887903}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-PEG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA].
-==Reference==
-Structural basis for the product specificity of histone lysine methyltransferases., Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X, Mol Cell. 2003 Jul;12(1):177-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12887903 12887903]
-[[Category: Histone-lysine N-methyltransferase]]
 [[Category: Neurospora crassa]]
-[[Category: Protein complex]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Cheng, X.]]
+[[Category: Cheng X]]
-[[Category: Horton, J R.]]
+[[Category: Horton JR]]
-[[Category: Khan, S I.]]
+[[Category: Khan SI]]
-[[Category: Selker, E U.]]
+[[Category: Selker EU]]
-[[Category: Tamaru, H.]]
+[[Category: Tamaru H]]
-[[Category: Yang, Z.]]
+[[Category: Yang Z]]
-[[Category: Zhang, X.]]
+[[Category: Zhang X]]
-[[Category: A hybrid beta sheet formed by dim-5 and h3 tail]]
-[[Category: A suv39-type histone-h3 lys-9 methyltransferase]]
-[[Category: Post-set zinc-binding site]]
-[[Category: Pre-set triangular zn3cys9 zinc cluster]]
-[[Category: Set domain protein forms a knot-like substructure]]
-[[Category: Ternary structure of dim-5]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:38:18 2008''