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| {{STRUCTURE_1n6a| PDB=1n6a | SCENE= }} | | {{STRUCTURE_1n6a| PDB=1n6a | SCENE= }} |
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| '''Structure of SET7/9'''
| | ===Structure of SET7/9=== |
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| ==Overview==
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| The methylation of lysine residues of histones plays a pivotal role in the regulation of chromatin structure and gene expression. Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution. The structures reveal an active site consisting of: (i) a binding pocket between the SET domain and a c-SET helix where an AdoMet molecule in an unusual conformation binds; (ii) a narrow substrate-specific channel that only unmethylated lysine residues can access; and (iii) a catalytic tyrosine residue. The methyl group of AdoMet is directed to the narrow channel where a substrate lysine enters from the opposite side. We demonstrate that SET7/9 can transfer two but not three methyl groups to unmodified Lys4 of H3 without substrate dissociation. The unusual features of the SET domain-containing HMTase discriminate between the un- and methylated lysine substrate, and the methylation sites for the histone H3 tail. | | The line below this paragraph, {{ABSTRACT_PUBMED_12514135}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12514135 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12514135}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lee, J.]] | | [[Category: Lee, J.]] |
| [[Category: Protein-ligand complex]] | | [[Category: Protein-ligand complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:08:54 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:13:06 2008'' |
