1ri5: Difference between revisions

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[[Image:1ri5.~~gif~~|left|200px]]

[[Image:1ri5.png|left|200px]]

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~~'''~~Structure and mechanism of mRNA cap (guanine N-7) methyltransferase~~'''~~

===Structure and mechanism of mRNA cap (guanine N-7) methyltransferase===

~~==Overview==~~

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~~A suite of crystal structures is reported for a cellular mRNA cap (guanine~~-~~N7) methyltransferase in complex with AdoMet, AdoHcy, and the cap guanylate. Superposition of ligand complexes suggests an in~~-line ~~mechanism of methyl transfer~~, ~~albeit without direct contacts between~~ the ~~enzyme and either~~ the ~~N7 atom of guanine~~ (~~the attacking nucleophile~~), ~~the methyl carbon of AdoMet, or the sulfur of AdoMet/AdoHcy (the leaving group). The structures indicate that catalysis of cap N7 methylation~~ is ~~accomplished by optimizing proximity and orientation of~~ the ~~substrates, assisted by a favorable electrostatic environment~~. ~~The enzyme~~-~~ligand structures, together with new mutational data, fully account for the biochemical specificity of the cap guanine~~-~~N7 methylation reaction, an essential and defining step of eukaryotic mRNA synthesis.~~

The line below this paragraph, {{ABSTRACT_PUBMED_14731396}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14731396 is the PubMed ID number.

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==About this Structure==

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[[Category: Rna]]

[[Category: Structural genomic]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3~~ 07:31:35 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:15:24 2008''

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-[[Image:1ri5.gif|left|200px]]
+{{Seed}}
+[[Image:1ri5.png|left|200px]]
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 {{STRUCTURE_1ri5|  PDB=1ri5  |  SCENE=  }}
-'''Structure and mechanism of mRNA cap (guanine N-7) methyltransferase'''
+===Structure and mechanism of mRNA cap (guanine N-7) methyltransferase===
-==Overview==
+<!--
-A suite of crystal structures is reported for a cellular mRNA cap (guanine-N7) methyltransferase in complex with AdoMet, AdoHcy, and the cap guanylate. Superposition of ligand complexes suggests an in-line mechanism of methyl transfer, albeit without direct contacts between the enzyme and either the N7 atom of guanine (the attacking nucleophile), the methyl carbon of AdoMet, or the sulfur of AdoMet/AdoHcy (the leaving group). The structures indicate that catalysis of cap N7 methylation is accomplished by optimizing proximity and orientation of the substrates, assisted by a favorable electrostatic environment. The enzyme-ligand structures, together with new mutational data, fully account for the biochemical specificity of the cap guanine-N7 methylation reaction, an essential and defining step of eukaryotic mRNA synthesis.
+The line below this paragraph, {{ABSTRACT_PUBMED_14731396}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14731396 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14731396}}
 ==About this Structure==
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 [[Category: Rna]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:31:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:15:24 2008''