1u2z

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[[Image:1u2z.gif|left|200px]]
 
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{{Structure
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==Crystal structure of histone K79 methyltransferase Dot1p from yeast==
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|PDB= 1u2z |SIZE=350|CAPTION= <scene name='initialview01'>1u2z</scene>, resolution 2.20&Aring;
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<StructureSection load='1u2z' size='340' side='right'caption='[[1u2z]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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<table><tr><td colspan='2'>[[1u2z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2Z FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43]
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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]] 2.2&#8491;</td></tr>
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|GENE= DOT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<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></td></tr>
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}}
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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=1u2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2z OCA], [https://pdbe.org/1u2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2z RCSB], [https://www.ebi.ac.uk/pdbsum/1u2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DOT1_YEAST DOT1_YEAST] Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro).<ref>PMID:9755194</ref> <ref>PMID:11029058</ref> <ref>PMID:12097318</ref> <ref>PMID:12152067</ref> <ref>PMID:12574507</ref> <ref>PMID:15632126</ref> <ref>PMID:16166626</ref> <ref>PMID:15292170</ref>
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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/u2/1u2z_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=1u2z ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of histone K79 methyltransferase Dot1p from yeast'''
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Methylation of Lys79 on histone H3 by Dot1p is important for gene silencing. The elongated structure of the conserved core of yeast Dot1p contains an N-terminal helical domain and a seven-stranded catalytic domain that harbors the binding site for the methyl-donor and an active site pocket sided with conserved hydrophobic residues. The S-adenosyl-L-homocysteine exhibits an extended conformation distinct from the folded conformation observed in structures of SET domain histone lysine methyltransferases. A catalytic asparagine (Asn479), located at the bottom of the active site pocket, suggests a mechanism similar to that employed for amino methylation in DNA and protein glutamine methylation. The acidic, concave cleft between the two domains contains two basic residue binding pockets that could accommodate the outwardly protruding basic side chains around Lys79 of histone H3 on the disk-like nucleosome surface. Biochemical studies suggest that recombinant Dot1 proteins are active on recombinant nucleosomes, free of any modifications.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1U2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2Z OCA].
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==Reference==
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Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase., Sawada K, Yang Z, Horton JR, Collins RE, Zhang X, Cheng X, J Biol Chem. 2004 Oct 8;279(41):43296-306. Epub 2004 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15292170 15292170]
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Cheng X]]
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[[Category: Cheng, X.]]
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[[Category: Collins RE]]
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[[Category: Collins, R E.]]
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[[Category: Horton JR]]
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[[Category: Horton, J R.]]
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[[Category: Sawada K]]
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[[Category: Sawada, K.]]
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[[Category: Yang Z]]
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[[Category: Yang, Z.]]
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[[Category: Zhang X]]
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[[Category: Zhang, X.]]
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[[Category: SAH]]
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[[Category: histone methyltransferase]]
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[[Category: nucleosome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:26:44 2008''
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Current revision

Crystal structure of histone K79 methyltransferase Dot1p from yeast

PDB ID 1u2z

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