1ml9
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ml9' size='340' side='right'caption='[[1ml9]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='1ml9' size='340' side='right'caption='[[1ml9]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ML9 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=1ml9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ml9 OCA], [https://pdbe.org/1ml9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ml9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ml9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ml9 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=1ml9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ml9 OCA], [https://pdbe.org/1ml9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ml9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ml9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ml9 ProSAT]</span></td></tr> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1ml9 ConSurf]. | </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=1ml9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain. | ||
| - | |||
| - | Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.,Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X Cell. 2002 Oct 4;111(1):117-27. PMID:12372305<ref>PMID:12372305</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ml9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Chrysonilia crassa]] | ||
| - | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cheng | + | [[Category: Neurospora crassa]] |
| - | [[Category: Horton | + | [[Category: Cheng X]] |
| - | [[Category: Keefe | + | [[Category: Horton JR]] |
| - | [[Category: Khan | + | [[Category: Keefe LJ]] |
| - | [[Category: Selker | + | [[Category: Khan SI]] |
| - | [[Category: Tamaru | + | [[Category: Selker EU]] |
| - | [[Category: Zhang | + | [[Category: Tamaru H]] |
| - | + | [[Category: Zhang X]] | |
| - | + | ||
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Revision as of 07:45, 14 February 2024
Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase
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Categories: Large Structures | Neurospora crassa | Cheng X | Horton JR | Keefe LJ | Khan SI | Selker EU | Tamaru H | Zhang X
