1u2z: Difference between revisions

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<StructureSection load='1u2z' size='340' side='right'caption='[[1u2z]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1u2z' size='340' side='right'caption='[[1u2z]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1u2z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1U2Z FirstGlance]. <br>
<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>
</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></td></tr>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DOT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2z OCA], [http://pdbe.org/1u2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u2z RCSB], [http://www.ebi.ac.uk/pdbsum/1u2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
== 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=1u2z 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=1u2z ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:15292170<ref>PMID:15292170</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1u2z" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cheng, X]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Collins, R E]]
[[Category: Cheng X]]
[[Category: Horton, J R]]
[[Category: Collins RE]]
[[Category: Sawada, K]]
[[Category: Horton JR]]
[[Category: Yang, Z]]
[[Category: Sawada K]]
[[Category: Zhang, X]]
[[Category: Yang Z]]
[[Category: Histone methyltransferase]]
[[Category: Zhang X]]
[[Category: Nucleosome]]
[[Category: Transferase]]
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