1n6c
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1n6c.jpg|left|200px]] | + | [[Image:1n6c.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of SET7/9''' | + | {{Structure |
| + | |PDB= 1n6c |SIZE=350|CAPTION= <scene name='initialview01'>1n6c</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of SET7/9''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1N6C is a [ | + | 1N6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6C OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12514135 12514135] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:43 2008'' |
Revision as of 10:52, 20 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of SET7/9
Overview
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.
About this Structure
1N6C 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
Page seeded by OCA on Thu Mar 20 12:52:43 2008
