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4bup
From Proteopedia
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==A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases== | ==A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases== | ||
| - | <StructureSection load='4bup' size='340' side='right' caption='[[4bup]], [[Resolution|resolution]] 2.17Å' scene=''> | + | <StructureSection load='4bup' size='340' side='right'caption='[[4bup]], [[Resolution|resolution]] 2.17Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4bup]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4bup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUP FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.166Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4bup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bup OCA], [https://pdbe.org/4bup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bup RCSB], [https://www.ebi.ac.uk/pdbsum/4bup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bup ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/KMT5B_MOUSE KMT5B_MOUSE] Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity (PubMed:28114273, PubMed:24049080, PubMed:15145825). In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression (PubMed:15145825). Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions (PubMed:15145825). KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (PubMed:16612004, PubMed:15750587). Plays a role in myogenesis by regulating the expression of target genes, such as EID3 (PubMed:23720823). Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (PubMed:28114273).[UniProtKB:Q4FZB7]<ref>PMID:15145825</ref> <ref>PMID:15750587</ref> <ref>PMID:16612004</ref> <ref>PMID:23720823</ref> <ref>PMID:24049080</ref> <ref>PMID:28114273</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4bup" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Cronin | + | [[Category: Cronin NB]] |
| - | [[Category: Southall | + | [[Category: Southall SM]] |
| - | [[Category: Wilson | + | [[Category: Wilson JR]] |
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Current revision
A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases
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