4c1q: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{STRUCTURE_4c1q|  PDB=4c1q  |  SCENE=  }}
-===Crystal structure of the PRDM9 SET domain in complex with H3K4me2 and AdoHcy.===
-{{ABSTRACT_PUBMED_24095733}}
-==Function==
+==Crystal structure of the PRDM9 SET domain in complex with H3K4me2 and AdoHcy.==
-[[http://www.uniprot.org/uniprot/PRDM9_MOUSE PRDM9_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase.
+<StructureSection load='4c1q' size='340' side='right'caption='[[4c1q]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4c1q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C1Q FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<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=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=4c1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1q OCA], [https://pdbe.org/4c1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c1q RCSB], [https://www.ebi.ac.uk/pdbsum/4c1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRDM9_MOUSE PRDM9_MOUSE] Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+PRDM9, a histone lysine methyltransferase, is a key determinant of the localization of meiotic recombination hot spots in humans and mice and the only vertebrate protein known to be involved in hybrid sterility. Here, we report the crystal structure of the PRDM9 methyltransferase domain in complex with a histone H3 peptide dimethylated on lysine 4 (H3K4me2) and S-adenosylhomocysteine (AdoHcy), which provides insights into the methyltransferase activity of PRDM proteins. We show that the genuine substrate of PRDM9 is histone H3 lysine 4 (H3K4) and that the enzyme possesses mono-, di-, and trimethylation activities. We also determined the crystal structure of PRDM9 in its autoinhibited state, which revealed a rearrangement of the substrate and cofactor binding sites by a concerted action of the pre-SET and post-SET domains, providing important insights into the regulatory mechanisms of histone lysine methyltransferase activity.
-==About this Structure==
+Molecular Basis for the Regulation of the H3K4 Methyltransferase Activity of PRDM9.,Wu H, Mathioudakis N, Diagouraga B, Dong A, Dombrovski L, Baudat F, Cusack S, de Massy B, Kadlec J Cell Rep. 2013 Oct 2. pii: S2211-1247(13)00476-2. doi:, 10.1016/j.celrep.2013.08.035. PMID:24095733<ref>PMID:24095733</ref>
-[[4c1q]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1Q OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:024095733</ref><references group="xtra"/><references/>
+</div>
-[[Category: Histone-lysine N-methyltransferase]]
+<div class="pdbe-citations 4c1q" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Cusack, S.]]
+[[Category: Cusack S]]
-[[Category: Kadlec, J.]]
+[[Category: Kadlec J]]
-[[Category: Mathioudakis, N.]]
+[[Category: Mathioudakis N]]
-[[Category: Histone methyltransferase]]
-[[Category: Set domain h3k4me3]]
-[[Category: Transferase-peptide complex]]