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[[Image:1nw3.jpg|left|200px]]<br /><applet load="1nw3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nw3, resolution 2.5&Aring;" />
'''Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase'''<br />


==Overview==
==Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase==
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.
<StructureSection load='1nw3' size='340' side='right'caption='[[1nw3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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.
== 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/nw/1nw3_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=1nw3 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW3 OCA].
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12628190 12628190]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Feng, Q.]]
[[Category: Feng Q]]
[[Category: Li, Z.H.]]
[[Category: Li ZH]]
[[Category: Min, J.R.]]
[[Category: Min JR]]
[[Category: Xu, R.M.]]
[[Category: Xu RM]]
[[Category: Zhang, Y.]]
[[Category: Zhang Y]]
[[Category: ACT]]
[[Category: SAM]]
[[Category: SO4]]
[[Category: hdot1]]
[[Category: histone lysine methyltransferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:31:19 2008''

Latest revision as of 08:00, 14 February 2024

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

1nw3, resolution 2.50Å

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