1av6: Difference between revisions

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{{STRUCTURE_1av6|  PDB=1av6  |  SCENE=  }}  
{{STRUCTURE_1av6|  PDB=1av6  |  SCENE=  }}  


'''VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M7G CAPPED RNA HEXAMER AND S-ADENOSYLHOMOCYSTEINE'''
===VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M7G CAPPED RNA HEXAMER AND S-ADENOSYLHOMOCYSTEINE===




==Overview==
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Sequence-nonspecific binding of RNA, recognition of a 7-methylguanosine 5' mRNA cap, and methylation of a nucleic acid backbone are three crucial and ubiquitous events in eukaryotic nucleic acid processing and function. These three events occur concurrently in the modification of vaccinia transcripts by the methyltransferase VP39. We report the crystal structure of a ternary complex comprising VP39, coenzyme product S-adenosylhomocysteine, and a 5' m7 G-capped, single-stranded RNA hexamer. This structure reveals a novel and general mechanism for sequence-non-specific recognition of the mRNA transcript in which the protein interacts solely with the sugar-phosphate backbone of a short, single-stranded RNA helix. This report represents the first direct and detailed view of a protein complexed with single-stranded RNA or 5'-capped mRNA.
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{{ABSTRACT_PUBMED_9660928}}


==About this Structure==
==About this Structure==
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[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Vaccinia]]
[[Category: Vaccinia]]
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Revision as of 17:39, 30 June 2008

File:1av6.png

Template:STRUCTURE 1av6

VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M7G CAPPED RNA HEXAMER AND S-ADENOSYLHOMOCYSTEINEVACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M7G CAPPED RNA HEXAMER AND S-ADENOSYLHOMOCYSTEINE

Template:ABSTRACT PUBMED 9660928

About this StructureAbout this Structure

1AV6 is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for sequence-nonspecific recognition of 5'-capped mRNA by a cap-modifying enzyme., Hodel AE, Gershon PD, Quiocho FA, Mol Cell. 1998 Feb;1(3):443-7. PMID:9660928

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