1peg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:42, 16 August 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1peg.gif|left|200px]]
 
-
{{Structure
+
==Structural basis for the product specificity of histone lysine methyltransferases==
-
|PDB= 1peg |SIZE=350|CAPTION= <scene name='initialview01'>1peg</scene>, resolution 2.59&Aring;
+
<StructureSection load='1peg' size='340' side='right'caption='[[1peg]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
<table><tr><td colspan='2'>[[1peg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEG FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peg OCA], [https://pdbe.org/1peg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1peg RCSB], [https://www.ebi.ac.uk/pdbsum/1peg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1peg ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[1ml9|1ML9]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peg OCA], [http://www.ebi.ac.uk/pdbsum/1peg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1peg RCSB]</span>
+
== 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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1peg_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<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/main_output.php?pdb_ID=1peg ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
DIM-5 is a SUV39-type histone H3 Lys9 methyltransferase that is essential for DNA methylation in N. crassa. We report the structure of a ternary complex including DIM-5, S-adenosyl-L-homocysteine, and a substrate H3 peptide. The histone tail inserts as a parallel strand between two DIM-5 strands, completing a hybrid sheet. Three post-SET cysteines coordinate a zinc atom together with Cys242 from the SET signature motif (NHXCXPN) near the active site. Consequently, a narrow channel is formed to accommodate the target Lys9 side chain. The sulfur atom of S-adenosyl-L-homocysteine, where the transferable methyl group is to be attached in S-adenosyl-L-methionine, lies at the opposite end of the channel, approximately 4 A away from the target Lys9 nitrogen. Structural comparison of the active sites of DIM-5, an H3 Lys9 trimethyltransferase, and SET7/9, an H3 Lys4 monomethyltransferase, allowed us to design substitutions in both enzymes that profoundly alter their product specificities without affecting their catalytic activities.
-
'''Structural basis for the product specificity of histone lysine methyltransferases'''
+
Structural basis for the product specificity of histone lysine methyltransferases.,Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X Mol Cell. 2003 Jul;12(1):177-85. PMID:12887903<ref>PMID:12887903</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1peg" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
DIM-5 is a SUV39-type histone H3 Lys9 methyltransferase that is essential for DNA methylation in N. crassa. We report the structure of a ternary complex including DIM-5, S-adenosyl-L-homocysteine, and a substrate H3 peptide. The histone tail inserts as a parallel strand between two DIM-5 strands, completing a hybrid sheet. Three post-SET cysteines coordinate a zinc atom together with Cys242 from the SET signature motif (NHXCXPN) near the active site. Consequently, a narrow channel is formed to accommodate the target Lys9 side chain. The sulfur atom of S-adenosyl-L-homocysteine, where the transferable methyl group is to be attached in S-adenosyl-L-methionine, lies at the opposite end of the channel, approximately 4 A away from the target Lys9 nitrogen. Structural comparison of the active sites of DIM-5, an H3 Lys9 trimethyltransferase, and SET7/9, an H3 Lys4 monomethyltransferase, allowed us to design substitutions in both enzymes that profoundly alter their product specificities without affecting their catalytic activities.
+
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1PEG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Structural basis for the product specificity of histone lysine methyltransferases., Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X, Mol Cell. 2003 Jul;12(1):177-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12887903 12887903]
+
-
[[Category: Histone-lysine N-methyltransferase]]
+
[[Category: Neurospora crassa]]
[[Category: Neurospora crassa]]
-
[[Category: Protein complex]]
+
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Cheng, X.]]
+
[[Category: Cheng X]]
-
[[Category: Horton, J R.]]
+
[[Category: Horton JR]]
-
[[Category: Khan, S I.]]
+
[[Category: Khan SI]]
-
[[Category: Selker, E U.]]
+
[[Category: Selker EU]]
-
[[Category: Tamaru, H.]]
+
[[Category: Tamaru H]]
-
[[Category: Yang, Z.]]
+
[[Category: Yang Z]]
-
[[Category: Zhang, X.]]
+
[[Category: Zhang X]]
-
[[Category: a hybrid beta sheet formed by dim-5 and h3 tail]]
+
-
[[Category: a suv39-type histone-h3 lys-9 methyltransferase]]
+
-
[[Category: post-set zinc-binding site]]
+
-
[[Category: pre-set triangular zn3cys9 zinc cluster]]
+
-
[[Category: set domain protein forms a knot-like substructure]]
+
-
[[Category: ternary structure of dim-5]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:33 2008''
+

Current revision

Structural basis for the product specificity of histone lysine methyltransferases

PDB ID 1peg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1peg"
Personal tools