3ru0

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==Cocrystal structure of human SMYD3 with inhibitor Sinefungin bound==
==Cocrystal structure of human SMYD3 with inhibitor Sinefungin bound==
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<StructureSection load='3ru0' size='340' side='right' caption='[[3ru0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='3ru0' size='340' side='right'caption='[[3ru0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ru0]] is a 2 chain structure with 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=3RU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RU0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ru0]] is a 2 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=3RU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RU0 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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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]] 1.849&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMYD3, ZMYND1, ZNFN3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><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>
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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=3ru0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru0 OCA], [https://pdbe.org/3ru0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ru0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ru0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ru0 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ru0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ru0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ru0 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
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== Publication Abstract from PubMed ==
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The SET and MYND Domain (SMYD) proteins comprise a unique family of multi-domain SET histone methyltransferases that are implicated in human cancer progression. Here we report an analysis of the crystal structure of the full length human SMYD3 in a complex with an analog of the S-adenosyl methionine (SAM) methyl donor cofactor. The structure revealed an overall compact architecture in which the "split-SET" domain adopts a canonical SET domain fold and closely assembles with a Zn-binding MYND domain and a C-terminal superhelical 9 alpha-helical bundle similar to that observed for the mouse SMYD1 structure. Together, these structurally interlocked domains impose a highly confined binding pocket for histone substrates, suggesting a regulated mechanism for its enzymatic activity. Our mutational and biochemical analyses confirm regulatory roles of the unique structural elements both inside and outside the core SET domain and establish a previously undetected preference for trimethylation of H4K20.
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Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3.,Foreman KW, Brown M, Park F, Emtage S, Harriss J, Das C, Zhu L, Crew A, Arnold L, Shaaban S, Tucker P PLoS One. 2011;6(7):e22290. Epub 2011 Jul 14. PMID:21779408<ref>PMID:21779408</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arnold, L.]]
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[[Category: Large Structures]]
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[[Category: Brown, M.]]
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[[Category: Arnold L]]
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[[Category: Crew, A.]]
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[[Category: Brown M]]
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[[Category: Das, C.]]
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[[Category: Crew A]]
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[[Category: Emtage, S.]]
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[[Category: Das C]]
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[[Category: Foreman, K W.]]
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[[Category: Emtage S]]
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[[Category: Harriss, J.]]
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[[Category: Foreman KW]]
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[[Category: Park, F.]]
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[[Category: Harriss J]]
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[[Category: Shaaban, S.]]
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[[Category: Park F]]
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[[Category: Tucker, P.]]
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[[Category: Shaaban S]]
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[[Category: Zhu, L.]]
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[[Category: Tucker P]]
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[[Category: Methyltransferase]]
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[[Category: Zhu L]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Cocrystal structure of human SMYD3 with inhibitor Sinefungin bound

PDB ID 3ru0

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