1n6a: Difference between revisions
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|PDB= 1n6a |SIZE=350|CAPTION= <scene name='initialview01'>1n6a</scene>, resolution 1.70Å | |PDB= 1n6a |SIZE=350|CAPTION= <scene name='initialview01'>1n6a</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1n6c|1N6C]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6a OCA], [http://www.ebi.ac.uk/pdbsum/1n6a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n6a RCSB]</span> | |||
}} | }} | ||
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[[Category: Lee, C W.]] | [[Category: Lee, C W.]] | ||
[[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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:58 2008'' | ||
Revision as of 22:25, 30 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1N6C
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of SET7/9
OverviewOverview
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 StructureAbout this Structure
1N6A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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