1nw3

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[[Image:1nw3.jpg|left|200px]]
 
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{{Structure
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==Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase==
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|PDB= 1nw3 |SIZE=350|CAPTION= <scene name='initialview01'>1nw3</scene>, resolution 2.5&Aring;
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<StructureSection load='1nw3' size='340' side='right'caption='[[1nw3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1nw3]] 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=1NW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NW3 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE= dot1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw3 OCA], [https://pdbe.org/1nw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nw3 RCSB], [https://www.ebi.ac.uk/pdbsum/1nw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw3 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw3 OCA], [http://www.ebi.ac.uk/pdbsum/1nw3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nw3 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nw3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1nw3 ConSurf].
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<div style="clear:both"></div>
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'''Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase'''
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Dot1 is an evolutionarily conserved histone methyltransferase that methylates lysine-79 of histone H3 in the core domain. Unlike other histone methyltransferases, Dot1 does not contain a SET domain, and it specifically methylates nucleosomal histone H3. We have solved a 2.5 A resolution structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM). The structure reveals a unique organization of a mainly alpha-helical N-terminal domain and a central open alpha/beta structure, an active site consisting of a SAM binding pocket, and a potential lysine binding channel. We also show that a flexible, positively charged region at the C terminus of the catalytic domain is critical for nucleosome binding and enzymatic activity. These structural and biochemical analyses, combined with molecular modeling, provide mechanistic insights into the catalytic mechanism and nucleosomal specificity of Dot1 proteins.
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==About this Structure==
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1NW3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW3 OCA].
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==Reference==
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Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase., Min J, Feng Q, Li Z, Zhang Y, Xu RM, Cell. 2003 Mar 7;112(5):711-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12628190 12628190]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Feng, Q.]]
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[[Category: Feng Q]]
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[[Category: Li, Z H.]]
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[[Category: Li ZH]]
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[[Category: Min, J R.]]
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[[Category: Min JR]]
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[[Category: Xu, R M.]]
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[[Category: Xu RM]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: hdot1]]
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[[Category: histone lysine methyltransferase,]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:18 2008''
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Current revision

Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase

PDB ID 1nw3

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