1mvx

From Proteopedia

(Difference between revisions)

Revision as of 10:13, 25 October 2017

structure of the SET domain histone lysine methyltransferase Clr4

Structural highlights

1mvx is a 1 chain structure with sequence from Cbs 356. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1mvh
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Methylation of histone H3 lysine 9 is an important component of the 'histone code' for heterochromatic gene silencing. The SET domain-containing Clr4 protein, a close relative of Su(var)3-9 proteins in higher eukaryotes, specifically methylates lysine 9 of histone H3 and is essential for silencing in Schizosaccharomyces pombe. Here we report the 2.3 A resolution crystal structure of the catalytic domain of Clr4. The structure reveals an overall fold rich in beta-strands, a potential active site consisting of a SAM-binding pocket, and a connected groove that could accommodate the binding of the N-terminal tail of histone H3. The pre-SET motif contains a triangular zinc cluster coordinated by nine cysteines distant from the active site, whereas the post-SET region is largely flexible but proximal to the active site. The structure provides insights into the architecture of SET domain histone methyltransferases and establishes a paradigm for further characterization of the Clr4 family of epigenetic regulators.

Structure of the SET domain histone lysine methyltransferase Clr4.,Min J, Zhang X, Cheng X, Grewal SI, Xu RM Nat Struct Biol. 2002 Nov;9(11):828-32. PMID:12389037^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Horn PJ, Bastie JN, Peterson CL. A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation. Genes Dev. 2005 Jul 15;19(14):1705-14. PMID:16024659 doi:http://dx.doi.org/10.1101/gad.1328005
↑ Ekwall K, Ruusala T. Mutations in rik1, clr2, clr3 and clr4 genes asymmetrically derepress the silent mating-type loci in fission yeast. Genetics. 1994 Jan;136(1):53-64. PMID:8138176
↑ Min J, Zhang X, Cheng X, Grewal SI, Xu RM. Structure of the SET domain histone lysine methyltransferase Clr4. Nat Struct Biol. 2002 Nov;9(11):828-32. PMID:12389037 doi:http://dx.doi.org/10.1038/nsb860

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mvx"

@@ Line 1: / Line 1: @@
 ==structure of the SET domain histone lysine methyltransferase Clr4==
 <StructureSection load='1mvx' size='340' side='right' caption='[[1mvx]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mvh|1mvh]]</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=1mvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvx OCA], [http://pdbe.org/1mvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mvx RCSB], [http://www.ebi.ac.uk/pdbsum/1mvx PDBsum]</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=1mvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvx OCA], [http://pdbe.org/1mvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mvx RCSB], [http://www.ebi.ac.uk/pdbsum/1mvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvx ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mvx ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1mvx

From Proteopedia

Revision as of 10:13, 25 October 2017

structure of the SET domain histone lysine methyltransferase Clr4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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