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1n6a

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{{STRUCTURE_1n6a| PDB=1n6a | SCENE= }}
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'''Structure of SET7/9'''
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===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.
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==About this Structure==
==About this Structure==
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[[Category: Lee, J.]]
[[Category: Lee, J.]]
[[Category: Protein-ligand complex]]
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Revision as of 23:13, 28 July 2008

Image:1n6a.png

Template:STRUCTURE 1n6a

Structure of SET7/9

Template:ABSTRACT PUBMED 12514135

About this Structure

1N6A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet., Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y, EMBO J. 2003 Jan 15;22(2):292-303. PMID:12514135

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