1peg: Difference between revisions

Revision as of 13:38, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1peg.png

Template:STRUCTURE 1peg

Structural basis for the product specificity of histone lysine methyltransferasesStructural basis for the product specificity of histone lysine methyltransferases

Template:ABSTRACT PUBMED 12887903

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 Tue Jul 29 13:38:18 2008

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OCA

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-'''Structural basis for the product specificity of histone lysine methyltransferases'''
+===Structural basis for the product specificity of histone lysine methyltransferases===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12887903}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12887903 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12887903}}
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 [[Category: Set domain protein forms a knot-like substructure]]
 [[Category: Ternary structure of dim-5]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:38:18 2008''