3mag

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{{STRUCTURE_3mag| PDB=3mag | SCENE= }}
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'''VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE'''
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===VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE===
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==Overview==
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We have determined, by high resolution x-ray analysis, 10 structures comprising the mRNA cap-specific methyltransferase VP39 or specific mutants thereof in the presence of methylated nucleobase analogs (N1-methyladenine, N3-methyladenine, N1-methylcytosine, N3-methylcytosine) and their unmethylated counterparts, or nucleoside N7-methylguanosine. Together with solution affinity studies and previous crystallographic data for N7-methylguanosine and its phosphorylated derivatives, these data demonstrate that only methylated, positively charged bases are bound, indicating that their enhanced stacking with two aromatic side chains of VP39 (Tyr 22 and Phe 180) plays a dominant role in cap recognition. Four key features characterize this stacking interaction: (i) near perfect parallel alignment between the sandwiched methylated bases and aromatic side chains, (ii) substantial areas of overlap in the two-stacked rings, (iii) a 3.4-A interplanar spacing within the overlapping region, and (iv) positive charge in the heterocyclic nucleobase.
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{{ABSTRACT_PUBMED_10377383}}
==About this Structure==
==About this Structure==
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[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Vaccinia]]
[[Category: Vaccinia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:54:52 2008''

Revision as of 09:54, 3 July 2008

Image:3mag.png

Template:STRUCTURE 3mag

VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE

Template:ABSTRACT PUBMED 10377383

About this Structure

3MAG is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

Reference

mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains., Hu G, Gershon PD, Hodel AE, Quiocho FA, Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7149-54. PMID:10377383

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