1ml9

From Proteopedia

(Difference between revisions)

Current revision

Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase

Structural highlights

1ml9 is a 1 chain structure with sequence from Neurospora crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.98Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DIM5_NEUCR Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.^[1] ^[2] ^[3] ^[4]

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

AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain.

Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.,Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X Cell. 2002 Oct 4;111(1):117-27. PMID:12372305^[5]

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

References

↑ Tamaru H, Selker EU. A histone H3 methyltransferase controls DNA methylation in Neurospora crassa. Nature. 2001 Nov 15;414(6861):277-83. PMID:11713521 doi:http://dx.doi.org/10.1038/35104508
↑ Tamaru H, Zhang X, McMillen D, Singh PB, Nakayama J, Grewal SI, Allis CD, Cheng X, Selker EU. Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa. Nat Genet. 2003 May;34(1):75-9. PMID:12679815 doi:http://dx.doi.org/10.1038/ng1143
↑ Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell. 2002 Oct 4;111(1):117-27. PMID:12372305
↑ Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X. Structural basis for the product specificity of histone lysine methyltransferases. Mol Cell. 2003 Jul;12(1):177-85. PMID:12887903
↑ Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell. 2002 Oct 4;111(1):117-27. PMID:12372305

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ml9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ml9' size='340' side='right'caption='[[1ml9]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ML9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ML9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1ml9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ml9 OCA], [https://pdbe.org/1ml9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ml9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ml9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ml9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/DIM5_NEUCR DIM5_NEUCR] Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.<ref>PMID:11713521</ref> <ref>PMID:12679815</ref> <ref>PMID:12372305</ref> <ref>PMID:12887903</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1ml9_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Chrysonilia crassa]]
-[[Category: Histone-lysine N-methyltransferase]]
 [[Category: Large Structures]]
-[[Category: Cheng, X]]
+[[Category: Neurospora crassa]]
-[[Category: Horton, J R]]
+[[Category: Cheng X]]
-[[Category: Keefe, L J]]
+[[Category: Horton JR]]
-[[Category: Khan, S I]]
+[[Category: Keefe LJ]]
-[[Category: Selker, E U]]
+[[Category: Khan SI]]
-[[Category: Tamaru, H]]
+[[Category: Selker EU]]
-[[Category: Zhang, X]]
+[[Category: Tamaru H]]
-[[Category: Adomet-dependent methyltransferase histone h3 lysine-9 methylation]]
+[[Category: Zhang X]]
-[[Category: Dim-5]]
-[[Category: Transferase]]

1ml9

From Proteopedia

Current revision

Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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