1peg: Difference between revisions

Revision as of 04:59, 3 May 2008

Structural basis for the product specificity of histone lysine methyltransferases

OverviewOverview

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.

About this StructureAbout this Structure

1PEG is a Protein complex structure of sequences from Neurospora crassa. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 04:59:39 2008

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OCA

@@ Line 1: / Line 1: @@
 [[Image:1peg.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1peg |SIZE=350|CAPTION= <scene name='initialview01'>1peg</scene>, resolution 2.59&Aring;
+The line below this paragraph, containing "STRUCTURE_1peg", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|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>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1peg|  PDB=1peg  |  SCENE=  }}
-|RELATEDENTRY=[[1ml9|1ML9]]
-|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>
-}}
 '''Structural basis for the product specificity of histone lysine methyltransferases'''
@@ Line 33: / Line 30: @@
 [[Category: Yang, Z.]]
 [[Category: Zhang, X.]]
-[[Category: a hybrid beta sheet formed by dim-5 and h3 tail]]
+[[Category: A hybrid beta sheet formed by dim-5 and h3 tail]]
-[[Category: a suv39-type histone-h3 lys-9 methyltransferase]]
+[[Category: A suv39-type histone-h3 lys-9 methyltransferase]]
-[[Category: post-set zinc-binding site]]
+[[Category: Post-set zinc-binding site]]
-[[Category: pre-set triangular zn3cys9 zinc cluster]]
+[[Category: Pre-set triangular zn3cys9 zinc cluster]]
-[[Category: set domain protein forms a knot-like substructure]]
+[[Category: Set domain protein forms a knot-like substructure]]
-[[Category: ternary structure of dim-5]]
+[[Category: Ternary structure of dim-5]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:59:39 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:33 2008''