1n6a: Difference between revisions

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[[Image:1n6a.gif|left|200px]]<br />

[[Image:1n6a.gif|left|200px]]<br /><applet load="1n6a" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1n6a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1n6a, resolution 1.70Å" />

'''Structure of SET7/9'''<br />

==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.

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==

1N6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1N6A OCA].

1N6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6A OCA].

==Reference==

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Line 13:

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Chang, J.H.]]

[[Category: Chang, J H.]]

[[Category: Cho, Y.]]

[[Category: Joachimiak, A.]]

[[Category: Kim, Y.C.]]

[[Category: Kim, Y C.]]

[[Category: Kwak, E.]]

[[Category: Kwon, T.W.]]

[[Category: Kwon, T W.]]

[[Category: Lee, C.W.]]

[[Category: Lee, C W.]]

[[Category: Lee, J.]]

[[Category: SAM]]

[[Category: protein-ligand complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:18:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1n6a.gif|left|200px]]<br />
+[[Image:1n6a.gif|left|200px]]<br /><applet load="1n6a" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1n6a" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1n6a, resolution 1.70&Aring;" />
 '''Structure of SET7/9'''<br />
 ==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.
+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==
-N6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N6A OCA].
+N6A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6A OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Chang, J.H.]]
+[[Category: Chang, J H.]]
 [[Category: Cho, Y.]]
 [[Category: Joachimiak, A.]]
-[[Category: Kim, Y.C.]]
+[[Category: Kim, Y C.]]
 [[Category: Kwak, E.]]
-[[Category: Kwon, T.W.]]
+[[Category: Kwon, T W.]]
-[[Category: Lee, C.W.]]
+[[Category: Lee, C W.]]
 [[Category: Lee, J.]]
 [[Category: SAM]]
 [[Category: protein-ligand complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:18:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:43 2008''