5v2n

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==Crystal Structure of APO Human SETD8==
==Crystal Structure of APO Human SETD8==
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<StructureSection load='5v2n' size='340' side='right' caption='[[5v2n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5v2n' size='340' side='right'caption='[[5v2n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5v2n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V2N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5v2n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V2N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KMT5A, PRSET7, SET07, SET8, SETD8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2n OCA], [http://pdbe.org/5v2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v2n RCSB], [http://www.ebi.ac.uk/pdbsum/5v2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2n ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2n OCA], [http://pdbe.org/5v2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v2n RCSB], [http://www.ebi.ac.uk/pdbsum/5v2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KMT5A_HUMAN KMT5A_HUMAN]] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:23478445</ref>
[[http://www.uniprot.org/uniprot/KMT5A_HUMAN KMT5A_HUMAN]] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:23478445</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Elucidating the conformational heterogeneity of proteins is essential for understanding protein function and developing exogenous ligands. With the rapid development of experimental and computational methods, it is of great interest to integrate these approaches to illuminate the conformational landscapes of target proteins. SETD8 is a protein lysine methyltransferase (PKMT), which functions in vivo via the methylation of histone and nonhistone targets. Utilizing covalent inhibitors and depleting native ligands to trap hidden conformational states, we obtained diverse X-ray structures of SETD8. These structures were used to seed distributed atomistic molecular dynamics simulations that generated a total of six milliseconds of trajectory data. Markov state models, built via an automated machine learning approach and corroborated experimentally, reveal how slow conformational motions and conformational states are relevant to catalysis. These findings provide molecular insight on enzymatic catalysis and allosteric mechanisms of a PKMT via its detailed conformational landscape.
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The dynamic conformational landscape of the protein methyltransferase SETD8.,Chen S, Wiewiora RP, Meng F, Babault N, Ma A, Yu W, Qian K, Hu H, Zou H, Wang J, Fan S, Blum G, Pittella-Silva F, Beauchamp KA, Tempel W, Jiang H, Chen K, Skene RJ, Zheng YG, Brown PJ, Jin J, Luo C, Chodera JD, Luo M Elife. 2019 May 13;8. pii: 45403. doi: 10.7554/eLife.45403. PMID:31081496<ref>PMID:31081496</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5v2n" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone methyltransferase|Histone methyltransferase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Skene, R J]]
[[Category: Skene, R J]]
[[Category: Methyl transferase]]
[[Category: Methyl transferase]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 06:06, 12 June 2019

Crystal Structure of APO Human SETD8

PDB ID 5v2n

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