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1ri5

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{{STRUCTURE_1ri5| PDB=1ri5 | SCENE= }}
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'''Structure and mechanism of mRNA cap (guanine N-7) methyltransferase'''
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===Structure and mechanism of mRNA cap (guanine N-7) methyltransferase===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14731396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14731396}}
==About this Structure==
==About this Structure==
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[[Category: Rna]]
[[Category: Rna]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 04:15, 28 July 2008

Image:1ri5.png

Template:STRUCTURE 1ri5

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

Template:ABSTRACT PUBMED 14731396

About this Structure

1RI5 is a Single protein structure of sequence from Encephalitozoon cuniculi. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of mRNA cap (guanine-N7) methyltransferase., Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD, Mol Cell. 2004 Jan 16;13(1):77-89. PMID:14731396

Page seeded by OCA on Mon Jul 28 07:15:24 2008

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