1g6z

<StructureSection load='1g6z' size='340' side='right'caption='[[1g6z]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1g6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G6Z FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLR4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</td></tr>

[[https://www.uniprot.org/uniprot/CLR4_SCHPO CLR4_SCHPO]] Histone methyltransferase. Catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.<ref>PMID:16024659</ref> <ref>PMID:8138176</ref>

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== Publication Abstract from PubMed ==

The encapsulation of otherwise transcribable loci within transcriptionally inactive heterochromatin is rapidly gaining recognition as an important mechanism of epigenetic gene regulation. In the fission yeast Schizosaccharomyces pombe, heterochromatinization of the mat2/mat3 loci silences the mating-type information encoded within these loci. Here, we present the solution structure of the chromo domain from the cryptic loci regulator protein Clr4. Clr4 is known to regulate silencing and switching at the mating-type loci and to affect chromatin structure at centromeres. Clr4 and its human and Drosophila homologs have been identified as histone H3-specific methyltransferases, further implicating this family of proteins in chromatin remodeling. Our structure highlights a conserved surface that may be involved in chromo domain-ligand interactions. We have also analyzed two chromo domain mutants (W31G and W41G) that previously were shown to affect silencing and switching in full-length Clr4. Both mutants are significantly destabilized relative to wild-type.

Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4.,Horita DA, Ivanova AV, Altieri AS, Klar AJ, Byrd RA J Mol Biol. 2001 Mar 30;307(3):861-70. PMID:11273706<ref>PMID:11273706</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1g6z" style="background-color:#fffaf0;"></div>

[[Category: Cbs 356]]

[[Category: Altieri, A S]]

[[Category: Byrd, R A]]

[[Category: Horita, D A]]

[[Category: Ivanova, A V]]

[[Category: Klar, A J]]

[[Category: Transferase]]